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craf crd (136–188)  (ATUM Bio)

 
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    Structured Review

    ATUM Bio craf crd (136–188)
    Modeling of membrane-anchored <t>RBD-CRD.</t> (A) Domain structure of <t>CRAF.</t> (B) One of the sampled conformations of CRAF RBD-CRD in the simulations. All simulations were started with the CRD (orange cartoons) anchored to a membrane patch but with the RBD (green cartoons) initially positioned away from the the membrane. The membrane patch is shown here using atom-based coloring (blue for carbon, red for oxygen, orange for phosphorus, darker blue for nitrogen, and light gray for hydrogen). The conformation shown here corresponds to pose GH5 in (24), in which the RBD has approached the membrane surface while keeping the main RAS-interacting β-strand (red cartoons) accessible for binding to the RAS G domain. The two zinc ions coordinated with the CRD are shown as gray spheres.
    Craf Crd (136–188), supplied by ATUM Bio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/craf crd (136–188)/product/ATUM Bio
    Average 90 stars, based on 1 article reviews
    craf crd (136–188) - by Bioz Stars, 2026-04
    90/100 stars

    Images

    1) Product Images from "Anionic Lipids Impact RAS-Binding Site Accessibility and Membrane Binding Affinity of CRAF RBD-CRD"

    Article Title: Anionic Lipids Impact RAS-Binding Site Accessibility and Membrane Binding Affinity of CRAF RBD-CRD

    Journal: Biophysical Journal

    doi: 10.1016/j.bpj.2020.06.021

    Modeling of membrane-anchored RBD-CRD. (A) Domain structure of CRAF. (B) One of the sampled conformations of CRAF RBD-CRD in the simulations. All simulations were started with the CRD (orange cartoons) anchored to a membrane patch but with the RBD (green cartoons) initially positioned away from the the membrane. The membrane patch is shown here using atom-based coloring (blue for carbon, red for oxygen, orange for phosphorus, darker blue for nitrogen, and light gray for hydrogen). The conformation shown here corresponds to pose GH5 in (24), in which the RBD has approached the membrane surface while keeping the main RAS-interacting β-strand (red cartoons) accessible for binding to the RAS G domain. The two zinc ions coordinated with the CRD are shown as gray spheres.
    Figure Legend Snippet: Modeling of membrane-anchored RBD-CRD. (A) Domain structure of CRAF. (B) One of the sampled conformations of CRAF RBD-CRD in the simulations. All simulations were started with the CRD (orange cartoons) anchored to a membrane patch but with the RBD (green cartoons) initially positioned away from the the membrane. The membrane patch is shown here using atom-based coloring (blue for carbon, red for oxygen, orange for phosphorus, darker blue for nitrogen, and light gray for hydrogen). The conformation shown here corresponds to pose GH5 in (24), in which the RBD has approached the membrane surface while keeping the main RAS-interacting β-strand (red cartoons) accessible for binding to the RAS G domain. The two zinc ions coordinated with the CRD are shown as gray spheres.

    Techniques Used: Binding Assay

    Membrane orientations of the RBD from CG simulations of CRAF RBD-CRD. (A) Free energy surface map for RBD orientations relative to the membrane surface from the CG RBD-CRD simulations. The reaction coordinates along the two axes are described in the text. Two major basins can be seen from this map. (B) Representative snapshots of CG RBD-CRD configurations for the two basins identified in (A). Both CG frames were backmapped to show the secondary structure of RBD-CRD. The RBS of the RBD, comprising a β-strand at residues K65–N71 and the adjacent α-helix at residues K84–R89, are colored red. The left and right panels show the RBS located near the membrane surface or away from it, respectively. Also highlighted in the right panel is a CRAF loop homologous to an ARAF loop that was previously shown to associate with membranes in the presence of KRAS (32). (C) The relative ASA of the RBS in each CG frame is projected onto the surface map of both reaction coordinates from (A). (D) Percentage of total CG simulations frames that fall under particular ranges of relative ASA for the RBS.
    Figure Legend Snippet: Membrane orientations of the RBD from CG simulations of CRAF RBD-CRD. (A) Free energy surface map for RBD orientations relative to the membrane surface from the CG RBD-CRD simulations. The reaction coordinates along the two axes are described in the text. Two major basins can be seen from this map. (B) Representative snapshots of CG RBD-CRD configurations for the two basins identified in (A). Both CG frames were backmapped to show the secondary structure of RBD-CRD. The RBS of the RBD, comprising a β-strand at residues K65–N71 and the adjacent α-helix at residues K84–R89, are colored red. The left and right panels show the RBS located near the membrane surface or away from it, respectively. Also highlighted in the right panel is a CRAF loop homologous to an ARAF loop that was previously shown to associate with membranes in the presence of KRAS (32). (C) The relative ASA of the RBS in each CG frame is projected onto the surface map of both reaction coordinates from (A). (D) Percentage of total CG simulations frames that fall under particular ranges of relative ASA for the RBS.

    Techniques Used:

    Limited accessibility of the RBS on the RBD from AA simulations of CRAF RBD-CRD. (A) Free energy surface map for RBD orientations relative to the membrane surface from the AA RBD-CRD simulations, using the same two reaction coordinates as in Fig. 2A. The AA frames were filtered to include only those showing a z distance of 2 nm or less between the RBD COM and the membrane surface. Black vertical dashed line at x = 3.5 nm separates the two observed basins. (B) Normalized probability distribution for percentage volume overlap between KRAS4b G domain and the membrane, based on structural alignment of a homology model of the KRAS4b G domain-CRAF RBD complex and the AA RBD-CRD simulations. The x axis is binned with widths of 5%. A majority of the frames show volume overlaps of greater than 5% (orange columns); however, a separate peak occurs for small volume overlaps between 0 and 5% (blue column). (C) Normalized probability distributions of the z distance between the RAS-interacting β-strand COM and the membrane COM for AA frames showing low (<5%) volume overlap of RAS with the membrane (blue columns) and for AA frames showing high (>5%) volume overlap (orange columns). Black dashed line indicates that a z distance cutoff value of 3.5 nm can effectively distinguish between conformations that have the RBS accessible (low overlap) or inaccessible (high overlap). Error bars in (B) and (C) give SEM over 30 AA simulations.
    Figure Legend Snippet: Limited accessibility of the RBS on the RBD from AA simulations of CRAF RBD-CRD. (A) Free energy surface map for RBD orientations relative to the membrane surface from the AA RBD-CRD simulations, using the same two reaction coordinates as in Fig. 2A. The AA frames were filtered to include only those showing a z distance of 2 nm or less between the RBD COM and the membrane surface. Black vertical dashed line at x = 3.5 nm separates the two observed basins. (B) Normalized probability distribution for percentage volume overlap between KRAS4b G domain and the membrane, based on structural alignment of a homology model of the KRAS4b G domain-CRAF RBD complex and the AA RBD-CRD simulations. The x axis is binned with widths of 5%. A majority of the frames show volume overlaps of greater than 5% (orange columns); however, a separate peak occurs for small volume overlaps between 0 and 5% (blue column). (C) Normalized probability distributions of the z distance between the RAS-interacting β-strand COM and the membrane COM for AA frames showing low (<5%) volume overlap of RAS with the membrane (blue columns) and for AA frames showing high (>5%) volume overlap (orange columns). Black dashed line indicates that a z distance cutoff value of 3.5 nm can effectively distinguish between conformations that have the RBS accessible (low overlap) or inaccessible (high overlap). Error bars in (B) and (C) give SEM over 30 AA simulations.

    Techniques Used:



    Similar Products

    craf crd (136–188)  (ATUM Bio)
    90
    ATUM Bio craf crd (136–188)
    Modeling of membrane-anchored <t>RBD-CRD.</t> (A) Domain structure of <t>CRAF.</t> (B) One of the sampled conformations of CRAF RBD-CRD in the simulations. All simulations were started with the CRD (orange cartoons) anchored to a membrane patch but with the RBD (green cartoons) initially positioned away from the the membrane. The membrane patch is shown here using atom-based coloring (blue for carbon, red for oxygen, orange for phosphorus, darker blue for nitrogen, and light gray for hydrogen). The conformation shown here corresponds to pose GH5 in (24), in which the RBD has approached the membrane surface while keeping the main RAS-interacting β-strand (red cartoons) accessible for binding to the RAS G domain. The two zinc ions coordinated with the CRD are shown as gray spheres.
    Craf Crd (136–188), supplied by ATUM Bio, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/craf crd (136–188)/product/ATUM Bio
    Average 90 stars, based on 1 article reviews
    craf crd (136–188) - by Bioz Stars, 2026-04
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Modeling of membrane-anchored RBD-CRD. (A) Domain structure of CRAF. (B) One of the sampled conformations of CRAF RBD-CRD in the simulations. All simulations were started with the CRD (orange cartoons) anchored to a membrane patch but with the RBD (green cartoons) initially positioned away from the the membrane. The membrane patch is shown here using atom-based coloring (blue for carbon, red for oxygen, orange for phosphorus, darker blue for nitrogen, and light gray for hydrogen). The conformation shown here corresponds to pose GH5 in (24), in which the RBD has approached the membrane surface while keeping the main RAS-interacting β-strand (red cartoons) accessible for binding to the RAS G domain. The two zinc ions coordinated with the CRD are shown as gray spheres.

    Journal: Biophysical Journal

    Article Title: Anionic Lipids Impact RAS-Binding Site Accessibility and Membrane Binding Affinity of CRAF RBD-CRD

    doi: 10.1016/j.bpj.2020.06.021

    Figure Lengend Snippet: Modeling of membrane-anchored RBD-CRD. (A) Domain structure of CRAF. (B) One of the sampled conformations of CRAF RBD-CRD in the simulations. All simulations were started with the CRD (orange cartoons) anchored to a membrane patch but with the RBD (green cartoons) initially positioned away from the the membrane. The membrane patch is shown here using atom-based coloring (blue for carbon, red for oxygen, orange for phosphorus, darker blue for nitrogen, and light gray for hydrogen). The conformation shown here corresponds to pose GH5 in (24), in which the RBD has approached the membrane surface while keeping the main RAS-interacting β-strand (red cartoons) accessible for binding to the RAS G domain. The two zinc ions coordinated with the CRD are shown as gray spheres.

    Article Snippet: Cloning, protein expression, and protein purification Gateway Entry clones for CRAF constructs were synthesized using optimization for Escherichia coli or insect cells (ATUM, Newark, CA) that incorporate an upstream tobacco etch virus protease cleavage site (ENLYFQ/G) followed by the appropriate CRAF (human) sequences: CRAF RBD-CRD (52–192) wild-type (WT) and mutants (mts), CRAF RBD (52–131), and CRAF CRD (136–188).

    Techniques: Binding Assay

    Membrane orientations of the RBD from CG simulations of CRAF RBD-CRD. (A) Free energy surface map for RBD orientations relative to the membrane surface from the CG RBD-CRD simulations. The reaction coordinates along the two axes are described in the text. Two major basins can be seen from this map. (B) Representative snapshots of CG RBD-CRD configurations for the two basins identified in (A). Both CG frames were backmapped to show the secondary structure of RBD-CRD. The RBS of the RBD, comprising a β-strand at residues K65–N71 and the adjacent α-helix at residues K84–R89, are colored red. The left and right panels show the RBS located near the membrane surface or away from it, respectively. Also highlighted in the right panel is a CRAF loop homologous to an ARAF loop that was previously shown to associate with membranes in the presence of KRAS (32). (C) The relative ASA of the RBS in each CG frame is projected onto the surface map of both reaction coordinates from (A). (D) Percentage of total CG simulations frames that fall under particular ranges of relative ASA for the RBS.

    Journal: Biophysical Journal

    Article Title: Anionic Lipids Impact RAS-Binding Site Accessibility and Membrane Binding Affinity of CRAF RBD-CRD

    doi: 10.1016/j.bpj.2020.06.021

    Figure Lengend Snippet: Membrane orientations of the RBD from CG simulations of CRAF RBD-CRD. (A) Free energy surface map for RBD orientations relative to the membrane surface from the CG RBD-CRD simulations. The reaction coordinates along the two axes are described in the text. Two major basins can be seen from this map. (B) Representative snapshots of CG RBD-CRD configurations for the two basins identified in (A). Both CG frames were backmapped to show the secondary structure of RBD-CRD. The RBS of the RBD, comprising a β-strand at residues K65–N71 and the adjacent α-helix at residues K84–R89, are colored red. The left and right panels show the RBS located near the membrane surface or away from it, respectively. Also highlighted in the right panel is a CRAF loop homologous to an ARAF loop that was previously shown to associate with membranes in the presence of KRAS (32). (C) The relative ASA of the RBS in each CG frame is projected onto the surface map of both reaction coordinates from (A). (D) Percentage of total CG simulations frames that fall under particular ranges of relative ASA for the RBS.

    Article Snippet: Cloning, protein expression, and protein purification Gateway Entry clones for CRAF constructs were synthesized using optimization for Escherichia coli or insect cells (ATUM, Newark, CA) that incorporate an upstream tobacco etch virus protease cleavage site (ENLYFQ/G) followed by the appropriate CRAF (human) sequences: CRAF RBD-CRD (52–192) wild-type (WT) and mutants (mts), CRAF RBD (52–131), and CRAF CRD (136–188).

    Techniques:

    Limited accessibility of the RBS on the RBD from AA simulations of CRAF RBD-CRD. (A) Free energy surface map for RBD orientations relative to the membrane surface from the AA RBD-CRD simulations, using the same two reaction coordinates as in Fig. 2A. The AA frames were filtered to include only those showing a z distance of 2 nm or less between the RBD COM and the membrane surface. Black vertical dashed line at x = 3.5 nm separates the two observed basins. (B) Normalized probability distribution for percentage volume overlap between KRAS4b G domain and the membrane, based on structural alignment of a homology model of the KRAS4b G domain-CRAF RBD complex and the AA RBD-CRD simulations. The x axis is binned with widths of 5%. A majority of the frames show volume overlaps of greater than 5% (orange columns); however, a separate peak occurs for small volume overlaps between 0 and 5% (blue column). (C) Normalized probability distributions of the z distance between the RAS-interacting β-strand COM and the membrane COM for AA frames showing low (<5%) volume overlap of RAS with the membrane (blue columns) and for AA frames showing high (>5%) volume overlap (orange columns). Black dashed line indicates that a z distance cutoff value of 3.5 nm can effectively distinguish between conformations that have the RBS accessible (low overlap) or inaccessible (high overlap). Error bars in (B) and (C) give SEM over 30 AA simulations.

    Journal: Biophysical Journal

    Article Title: Anionic Lipids Impact RAS-Binding Site Accessibility and Membrane Binding Affinity of CRAF RBD-CRD

    doi: 10.1016/j.bpj.2020.06.021

    Figure Lengend Snippet: Limited accessibility of the RBS on the RBD from AA simulations of CRAF RBD-CRD. (A) Free energy surface map for RBD orientations relative to the membrane surface from the AA RBD-CRD simulations, using the same two reaction coordinates as in Fig. 2A. The AA frames were filtered to include only those showing a z distance of 2 nm or less between the RBD COM and the membrane surface. Black vertical dashed line at x = 3.5 nm separates the two observed basins. (B) Normalized probability distribution for percentage volume overlap between KRAS4b G domain and the membrane, based on structural alignment of a homology model of the KRAS4b G domain-CRAF RBD complex and the AA RBD-CRD simulations. The x axis is binned with widths of 5%. A majority of the frames show volume overlaps of greater than 5% (orange columns); however, a separate peak occurs for small volume overlaps between 0 and 5% (blue column). (C) Normalized probability distributions of the z distance between the RAS-interacting β-strand COM and the membrane COM for AA frames showing low (<5%) volume overlap of RAS with the membrane (blue columns) and for AA frames showing high (>5%) volume overlap (orange columns). Black dashed line indicates that a z distance cutoff value of 3.5 nm can effectively distinguish between conformations that have the RBS accessible (low overlap) or inaccessible (high overlap). Error bars in (B) and (C) give SEM over 30 AA simulations.

    Article Snippet: Cloning, protein expression, and protein purification Gateway Entry clones for CRAF constructs were synthesized using optimization for Escherichia coli or insect cells (ATUM, Newark, CA) that incorporate an upstream tobacco etch virus protease cleavage site (ENLYFQ/G) followed by the appropriate CRAF (human) sequences: CRAF RBD-CRD (52–192) wild-type (WT) and mutants (mts), CRAF RBD (52–131), and CRAF CRD (136–188).

    Techniques: