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α 2a ar goa complex  (New England Biolabs)


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    Structured Review

    New England Biolabs α 2a ar goa complex
    Cryo-EM density maps and models of the <t>α</t> <t>2A</t> AR-GoA complex bound to Norepi ( A ), BRI ( B ), DEX ( C ), and OXY ( D ). The densities of the agonists (shown as sticks) are depicted as gray meshes. The maps are colored according to different subunits.
    α 2a Ar Goa Complex, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 97/100, based on 565 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/%CE%B1+2a+ar+goa+complex/Apyrase/pmc08896805-184-1-13
    Average 97 stars, based on 565 article reviews
    α 2a ar goa complex - by Bioz Stars, 2026-09
    97/100 stars

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    1) Product Images from "Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor"

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor

    Journal: Science Advances

    doi: 10.1126/sciadv.abj5347

    Cryo-EM density maps and models of the α 2A AR-GoA complex bound to Norepi ( A ), BRI ( B ), DEX ( C ), and OXY ( D ). The densities of the agonists (shown as sticks) are depicted as gray meshes. The maps are colored according to different subunits.
    Figure Legend Snippet: Cryo-EM density maps and models of the α 2A AR-GoA complex bound to Norepi ( A ), BRI ( B ), DEX ( C ), and OXY ( D ). The densities of the agonists (shown as sticks) are depicted as gray meshes. The maps are colored according to different subunits.

    Techniques Used: Cryo-EM Sample Prep

    ( A ) Alignment of four structures of α 2A AR signaling complexes. ( B ) Superposition of Norepi, BRI, DEX, and OXY from cryo-EM structures. The imidazole moiety is highlighted by the dashed circle. ( C to F ) Detailed interactions of Norepi (C), BRI (D), DEX (E), and OXY (F) with α 2A AR. Residues within 4 Å of agonist are shown in sticks. The polar interactions are indicated by black dashed lines. ( G ) Superposition of the α 2A AR orthosteric binding pocket residues bound to four different agonists. ( H and I ) Concentration-response curves of different agonists for G protein activation (H) and β-arrestin-2 recruitment (I) for wild-type (wt) α 2A AR and receptor mutants D128 3.32 A, Y431 7.43 A, S215 5.42 A, and Y409 6.55 A, respectively. Except for the activation of D128 3.32 A, which is normalized to DEX for G protein activation and relative to basal for arrestin recruitment, receptor activation is shown relative to the maximum effect of Norepi. Data are presented as means ± SEM of 3 to 11 independent experiments with repeats in duplicate.
    Figure Legend Snippet: ( A ) Alignment of four structures of α 2A AR signaling complexes. ( B ) Superposition of Norepi, BRI, DEX, and OXY from cryo-EM structures. The imidazole moiety is highlighted by the dashed circle. ( C to F ) Detailed interactions of Norepi (C), BRI (D), DEX (E), and OXY (F) with α 2A AR. Residues within 4 Å of agonist are shown in sticks. The polar interactions are indicated by black dashed lines. ( G ) Superposition of the α 2A AR orthosteric binding pocket residues bound to four different agonists. ( H and I ) Concentration-response curves of different agonists for G protein activation (H) and β-arrestin-2 recruitment (I) for wild-type (wt) α 2A AR and receptor mutants D128 3.32 A, Y431 7.43 A, S215 5.42 A, and Y409 6.55 A, respectively. Except for the activation of D128 3.32 A, which is normalized to DEX for G protein activation and relative to basal for arrestin recruitment, receptor activation is shown relative to the maximum effect of Norepi. Data are presented as means ± SEM of 3 to 11 independent experiments with repeats in duplicate.

    Techniques Used: Cryo-EM Sample Prep, Binding Assay, Concentration Assay, Activation Assay

    ( A ) Detailed interactions of Norepi with β 1 AR [Protein Data Bank (PDB) code: 7BU6]. Residues within 4 Å of agonist are shown in sticks. The polar interactions are indicated by black dashed lines. ( B ) Superposition of orthosteric pockets of β 1 AR-Norepi and β 2 AR-Epi (epinephrine) (PDB code: 4LDO). ( C ) Detailed interactions of dopamine with D1R (PDB code: 7CKZ). The polar interactions are indicated by black dashed lines. ( D ) Superposition of orthosteric pockets of β 1 AR-Norepi and α 2A AR-Norepi. Residues within 4 Å of agonist are shown in sticks.
    Figure Legend Snippet: ( A ) Detailed interactions of Norepi with β 1 AR [Protein Data Bank (PDB) code: 7BU6]. Residues within 4 Å of agonist are shown in sticks. The polar interactions are indicated by black dashed lines. ( B ) Superposition of orthosteric pockets of β 1 AR-Norepi and β 2 AR-Epi (epinephrine) (PDB code: 4LDO). ( C ) Detailed interactions of dopamine with D1R (PDB code: 7CKZ). The polar interactions are indicated by black dashed lines. ( D ) Superposition of orthosteric pockets of β 1 AR-Norepi and α 2A AR-Norepi. Residues within 4 Å of agonist are shown in sticks.

    Techniques Used:

    ( A ) Structural comparison of inactive α 2A AR bound to RS79948 and active α 2A AR bound to Norepi, with changes highlighted as red arrows. The distance is calculated between positions of Cα of residue 6.29 in TM6. ( B ) Conformational changes within the orthosteric pocket are shown from the extracellular side, with changes highlighted as red arrows. ( C ) Cross sections of α 2A AR bound to antagonist and agonist are shown, with the interior in black and the exosite highlighted. ( D ) Concentration-response curves of F427 7.39 mutant for different agonists toward G protein activation and β-arrestin-2 recruitment. Data are presented as means ± SEM of 4 to 10 independent experiments with repeats in duplicate.
    Figure Legend Snippet: ( A ) Structural comparison of inactive α 2A AR bound to RS79948 and active α 2A AR bound to Norepi, with changes highlighted as red arrows. The distance is calculated between positions of Cα of residue 6.29 in TM6. ( B ) Conformational changes within the orthosteric pocket are shown from the extracellular side, with changes highlighted as red arrows. ( C ) Cross sections of α 2A AR bound to antagonist and agonist are shown, with the interior in black and the exosite highlighted. ( D ) Concentration-response curves of F427 7.39 mutant for different agonists toward G protein activation and β-arrestin-2 recruitment. Data are presented as means ± SEM of 4 to 10 independent experiments with repeats in duplicate.

    Techniques Used: Concentration Assay, Mutagenesis, Activation Assay

    ( A and B ) Superposition of the G protein coupling interfaces of α 2A AR-GoA, α 2B AR-GoA, and β 2 AR-Gs complexes, using receptor for alignment. ( C to H ) Detailed interactions of α 2A AR with Goα (C and D), α 2B AR with Goα (E and F), and β 2 AR with Gsα (G and H). The polar interactions are indicated by red dashed lines.
    Figure Legend Snippet: ( A and B ) Superposition of the G protein coupling interfaces of α 2A AR-GoA, α 2B AR-GoA, and β 2 AR-Gs complexes, using receptor for alignment. ( C to H ) Detailed interactions of α 2A AR with Goα (C and D), α 2B AR with Goα (E and F), and β 2 AR with Gsα (G and H). The polar interactions are indicated by red dashed lines.

    Techniques Used:

    Related Articles

    Cryo-EM Sample Prep:

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor
    Article Snippet: with heterotrimeric GoA was formed in a buffer composed of 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.1% DDM, 1 mM MgCl 2 , 10 μM GDP, and 100 μM agonist. .. The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner. .. After elution by adding 5 mM EDTA and Flag peptide (0.2 mg ml −1 ), the complex was concentrated and incubated with excess scFv16 for 1 hour on ice an

    Binding Assay:

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor
    Article Snippet: with heterotrimeric GoA was formed in a buffer composed of 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.1% DDM, 1 mM MgCl 2 , 10 μM GDP, and 100 μM agonist. .. The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner. .. After elution by adding 5 mM EDTA and Flag peptide (0.2 mg ml −1 ), the complex was concentrated and incubated with excess scFv16 for 1 hour on ice an

    Concentration Assay:

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor
    Article Snippet: with heterotrimeric GoA was formed in a buffer composed of 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.1% DDM, 1 mM MgCl 2 , 10 μM GDP, and 100 μM agonist. .. The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner. .. After elution by adding 5 mM EDTA and Flag peptide (0.2 mg ml −1 ), the complex was concentrated and incubated with excess scFv16 for 1 hour on ice an

    Activation Assay:

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor
    Article Snippet: with heterotrimeric GoA was formed in a buffer composed of 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.1% DDM, 1 mM MgCl 2 , 10 μM GDP, and 100 μM agonist. .. The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner. .. After elution by adding 5 mM EDTA and Flag peptide (0.2 mg ml −1 ), the complex was concentrated and incubated with excess scFv16 for 1 hour on ice an

    Mutagenesis:

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor
    Article Snippet: with heterotrimeric GoA was formed in a buffer composed of 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.1% DDM, 1 mM MgCl 2 , 10 μM GDP, and 100 μM agonist. .. The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner. .. After elution by adding 5 mM EDTA and Flag peptide (0.2 mg ml −1 ), the complex was concentrated and incubated with excess scFv16 for 1 hour on ice an

    Microscopy:

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor
    Article Snippet: with heterotrimeric GoA was formed in a buffer composed of 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.1% DDM, 1 mM MgCl 2 , 10 μM GDP, and 100 μM agonist. .. The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner. .. After elution by adding 5 mM EDTA and Flag peptide (0.2 mg ml −1 ), the complex was concentrated and incubated with excess scFv16 for 1 hour on ice an



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    α 2a ar goa complex  (New England Biolabs)
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    New England Biolabs α 2a ar goa complex
    Cryo-EM density maps and models of the <t>α</t> <t>2A</t> AR-GoA complex bound to Norepi ( A ), BRI ( B ), DEX ( C ), and OXY ( D ). The densities of the agonists (shown as sticks) are depicted as gray meshes. The maps are colored according to different subunits.
    α 2a Ar Goa Complex, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/%CE%B1+2a+ar+goa+complex/Apyrase/pmc08896805-184-1-13
    Average 97 stars, based on 1 article reviews
    α 2a ar goa complex - by Bioz Stars, 2026-09
    97/100 stars
    		  Buy from Supplier

    Image Search Results


    Cryo-EM density maps and models of the α 2A AR-GoA complex bound to Norepi ( A ), BRI ( B ), DEX ( C ), and OXY ( D ). The densities of the agonists (shown as sticks) are depicted as gray meshes. The maps are colored according to different subunits.

    Journal: Science Advances

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor

    doi: 10.1126/sciadv.abj5347

    Figure Lengend Snippet: Cryo-EM density maps and models of the α 2A AR-GoA complex bound to Norepi ( A ), BRI ( B ), DEX ( C ), and OXY ( D ). The densities of the agonists (shown as sticks) are depicted as gray meshes. The maps are colored according to different subunits.

    Article Snippet: The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner.

    Techniques: Cryo-EM Sample Prep

    ( A ) Alignment of four structures of α 2A AR signaling complexes. ( B ) Superposition of Norepi, BRI, DEX, and OXY from cryo-EM structures. The imidazole moiety is highlighted by the dashed circle. ( C to F ) Detailed interactions of Norepi (C), BRI (D), DEX (E), and OXY (F) with α 2A AR. Residues within 4 Å of agonist are shown in sticks. The polar interactions are indicated by black dashed lines. ( G ) Superposition of the α 2A AR orthosteric binding pocket residues bound to four different agonists. ( H and I ) Concentration-response curves of different agonists for G protein activation (H) and β-arrestin-2 recruitment (I) for wild-type (wt) α 2A AR and receptor mutants D128 3.32 A, Y431 7.43 A, S215 5.42 A, and Y409 6.55 A, respectively. Except for the activation of D128 3.32 A, which is normalized to DEX for G protein activation and relative to basal for arrestin recruitment, receptor activation is shown relative to the maximum effect of Norepi. Data are presented as means ± SEM of 3 to 11 independent experiments with repeats in duplicate.

    Journal: Science Advances

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor

    doi: 10.1126/sciadv.abj5347

    Figure Lengend Snippet: ( A ) Alignment of four structures of α 2A AR signaling complexes. ( B ) Superposition of Norepi, BRI, DEX, and OXY from cryo-EM structures. The imidazole moiety is highlighted by the dashed circle. ( C to F ) Detailed interactions of Norepi (C), BRI (D), DEX (E), and OXY (F) with α 2A AR. Residues within 4 Å of agonist are shown in sticks. The polar interactions are indicated by black dashed lines. ( G ) Superposition of the α 2A AR orthosteric binding pocket residues bound to four different agonists. ( H and I ) Concentration-response curves of different agonists for G protein activation (H) and β-arrestin-2 recruitment (I) for wild-type (wt) α 2A AR and receptor mutants D128 3.32 A, Y431 7.43 A, S215 5.42 A, and Y409 6.55 A, respectively. Except for the activation of D128 3.32 A, which is normalized to DEX for G protein activation and relative to basal for arrestin recruitment, receptor activation is shown relative to the maximum effect of Norepi. Data are presented as means ± SEM of 3 to 11 independent experiments with repeats in duplicate.

    Article Snippet: The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner.

    Techniques: Cryo-EM Sample Prep, Binding Assay, Concentration Assay, Activation Assay

    ( A ) Detailed interactions of Norepi with β 1 AR [Protein Data Bank (PDB) code: 7BU6]. Residues within 4 Å of agonist are shown in sticks. The polar interactions are indicated by black dashed lines. ( B ) Superposition of orthosteric pockets of β 1 AR-Norepi and β 2 AR-Epi (epinephrine) (PDB code: 4LDO). ( C ) Detailed interactions of dopamine with D1R (PDB code: 7CKZ). The polar interactions are indicated by black dashed lines. ( D ) Superposition of orthosteric pockets of β 1 AR-Norepi and α 2A AR-Norepi. Residues within 4 Å of agonist are shown in sticks.

    Journal: Science Advances

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor

    doi: 10.1126/sciadv.abj5347

    Figure Lengend Snippet: ( A ) Detailed interactions of Norepi with β 1 AR [Protein Data Bank (PDB) code: 7BU6]. Residues within 4 Å of agonist are shown in sticks. The polar interactions are indicated by black dashed lines. ( B ) Superposition of orthosteric pockets of β 1 AR-Norepi and β 2 AR-Epi (epinephrine) (PDB code: 4LDO). ( C ) Detailed interactions of dopamine with D1R (PDB code: 7CKZ). The polar interactions are indicated by black dashed lines. ( D ) Superposition of orthosteric pockets of β 1 AR-Norepi and α 2A AR-Norepi. Residues within 4 Å of agonist are shown in sticks.

    Article Snippet: The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner.

    Techniques:

    ( A ) Structural comparison of inactive α 2A AR bound to RS79948 and active α 2A AR bound to Norepi, with changes highlighted as red arrows. The distance is calculated between positions of Cα of residue 6.29 in TM6. ( B ) Conformational changes within the orthosteric pocket are shown from the extracellular side, with changes highlighted as red arrows. ( C ) Cross sections of α 2A AR bound to antagonist and agonist are shown, with the interior in black and the exosite highlighted. ( D ) Concentration-response curves of F427 7.39 mutant for different agonists toward G protein activation and β-arrestin-2 recruitment. Data are presented as means ± SEM of 4 to 10 independent experiments with repeats in duplicate.

    Journal: Science Advances

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor

    doi: 10.1126/sciadv.abj5347

    Figure Lengend Snippet: ( A ) Structural comparison of inactive α 2A AR bound to RS79948 and active α 2A AR bound to Norepi, with changes highlighted as red arrows. The distance is calculated between positions of Cα of residue 6.29 in TM6. ( B ) Conformational changes within the orthosteric pocket are shown from the extracellular side, with changes highlighted as red arrows. ( C ) Cross sections of α 2A AR bound to antagonist and agonist are shown, with the interior in black and the exosite highlighted. ( D ) Concentration-response curves of F427 7.39 mutant for different agonists toward G protein activation and β-arrestin-2 recruitment. Data are presented as means ± SEM of 4 to 10 independent experiments with repeats in duplicate.

    Article Snippet: The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner.

    Techniques: Concentration Assay, Mutagenesis, Activation Assay

    ( A and B ) Superposition of the G protein coupling interfaces of α 2A AR-GoA, α 2B AR-GoA, and β 2 AR-Gs complexes, using receptor for alignment. ( C to H ) Detailed interactions of α 2A AR with Goα (C and D), α 2B AR with Goα (E and F), and β 2 AR with Gsα (G and H). The polar interactions are indicated by red dashed lines.

    Journal: Science Advances

    Article Title: Structural insights into ligand recognition, activation, and signaling of the α 2A adrenergic receptor

    doi: 10.1126/sciadv.abj5347

    Figure Lengend Snippet: ( A and B ) Superposition of the G protein coupling interfaces of α 2A AR-GoA, α 2B AR-GoA, and β 2 AR-Gs complexes, using receptor for alignment. ( C to H ) Detailed interactions of α 2A AR with Goα (C and D), α 2B AR with Goα (E and F), and β 2 AR with Gsα (G and H). The polar interactions are indicated by red dashed lines.

    Article Snippet: The α 2A AR-GoA complex was then treated with 50 U of apyrase (NEB) on ice overnight and exchanged on an anti-Flag M1 column into a buffer containing 20 mM Hepes (pH 7.5), 100 mM NaCl, 0.0075% lauryl maltose neopentyl glycol (MNG, NG310 Anatrace), 0.0025% GDN (GDN101, Anatrace), 0.001% CHS, 100 μM agonist, and 2 mM CaCl 2 in a stepwise manner.

    Techniques: