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fzd2-crd-fc  (R&D Systems)


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    Structured Review

    R&D Systems fzd2-crd-fc
    (A) Binding kinetics between TcdB and receptors are measured by BLI. The calculated binding affinities of TcdB to the 2 receptors, under pH 7.5 or pH 5, are labeled above each diagram. This measurement was calculated based on 2 biological replicates with standard deviations listed for each sample (raw data in ). (B) The structure comparisons of the TcdB-CRD2 complex at pH 7.5 and the 2 states at pH 5. (C) The helices (α2 and α4) of CRD2 that interact with TcdB are colored for each state. Dashed curves label the <t>CRD-binding</t> groove. Stars label the CRD-binding loop. Dark gray color labels regions in α-helices 2 and 4 that lack the cryo-EM density. The buried surface areas, calculated based on the model for the complex of TcdB and CRD2 under pH 7.5, state 1 and state 2 are around 700, 150, and 80 Å 2 , respectively. (D) The movement of the β-sheet (residues 1,812–1,827) in the D97 region are shown and color coded for each state. Tyr1819 of TcdB and its interaction partner Pro485 of CSPG4 are shown. (E) The same region rotated 90° from Panel D. BLI, bio-layer interferometry; CRD, cysteine-rich domain; CRD2, cysteine-rich domain <t>of</t> <t>frizzled-2;</t> TcdB, Toxin B.
    Fzd2 Crd Fc, supplied by R&D Systems, 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/fzd2-crd-fc/product/R&D Systems
    Average 90 stars, based on 1 article reviews
    fzd2-crd-fc - by Bioz Stars, 2026-06
    90/100 stars

    Images

    1) Product Images from "Structural dynamics of receptor recognition and pH-induced dissociation of full-length Clostridioides difficile Toxin B"

    Article Title: Structural dynamics of receptor recognition and pH-induced dissociation of full-length Clostridioides difficile Toxin B

    Journal: PLoS Biology

    doi: 10.1371/journal.pbio.3001589

    (A) Binding kinetics between TcdB and receptors are measured by BLI. The calculated binding affinities of TcdB to the 2 receptors, under pH 7.5 or pH 5, are labeled above each diagram. This measurement was calculated based on 2 biological replicates with standard deviations listed for each sample (raw data in ). (B) The structure comparisons of the TcdB-CRD2 complex at pH 7.5 and the 2 states at pH 5. (C) The helices (α2 and α4) of CRD2 that interact with TcdB are colored for each state. Dashed curves label the CRD-binding groove. Stars label the CRD-binding loop. Dark gray color labels regions in α-helices 2 and 4 that lack the cryo-EM density. The buried surface areas, calculated based on the model for the complex of TcdB and CRD2 under pH 7.5, state 1 and state 2 are around 700, 150, and 80 Å 2 , respectively. (D) The movement of the β-sheet (residues 1,812–1,827) in the D97 region are shown and color coded for each state. Tyr1819 of TcdB and its interaction partner Pro485 of CSPG4 are shown. (E) The same region rotated 90° from Panel D. BLI, bio-layer interferometry; CRD, cysteine-rich domain; CRD2, cysteine-rich domain of frizzled-2; TcdB, Toxin B.
    Figure Legend Snippet: (A) Binding kinetics between TcdB and receptors are measured by BLI. The calculated binding affinities of TcdB to the 2 receptors, under pH 7.5 or pH 5, are labeled above each diagram. This measurement was calculated based on 2 biological replicates with standard deviations listed for each sample (raw data in ). (B) The structure comparisons of the TcdB-CRD2 complex at pH 7.5 and the 2 states at pH 5. (C) The helices (α2 and α4) of CRD2 that interact with TcdB are colored for each state. Dashed curves label the CRD-binding groove. Stars label the CRD-binding loop. Dark gray color labels regions in α-helices 2 and 4 that lack the cryo-EM density. The buried surface areas, calculated based on the model for the complex of TcdB and CRD2 under pH 7.5, state 1 and state 2 are around 700, 150, and 80 Å 2 , respectively. (D) The movement of the β-sheet (residues 1,812–1,827) in the D97 region are shown and color coded for each state. Tyr1819 of TcdB and its interaction partner Pro485 of CSPG4 are shown. (E) The same region rotated 90° from Panel D. BLI, bio-layer interferometry; CRD, cysteine-rich domain; CRD2, cysteine-rich domain of frizzled-2; TcdB, Toxin B.

    Techniques Used: Binding Assay, Labeling, Cryo-EM Sample Prep

    (A) TcdB (shown as a ribbon model) binds to the receptors (gray cartoon), CSPG4 and FZD2, before endosomal acidification. The proposed pore-forming helices of TcdB are shown as orange ribbon models. (B) TcdB dissociates from the receptors and the pore-forming helices rearrange. Gray arrows indicate the dissociation of TcdB. Orange arrows suggest the insertion of pore-forming helices into the endosomal membrane. CSPG4, chondroitin sulfate proteoglycan 4; FZD2, frizzled-2; TcdB, Toxin B.
    Figure Legend Snippet: (A) TcdB (shown as a ribbon model) binds to the receptors (gray cartoon), CSPG4 and FZD2, before endosomal acidification. The proposed pore-forming helices of TcdB are shown as orange ribbon models. (B) TcdB dissociates from the receptors and the pore-forming helices rearrange. Gray arrows indicate the dissociation of TcdB. Orange arrows suggest the insertion of pore-forming helices into the endosomal membrane. CSPG4, chondroitin sulfate proteoglycan 4; FZD2, frizzled-2; TcdB, Toxin B.

    Techniques Used: Membrane



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    (A) Binding kinetics between TcdB and receptors are measured by BLI. The calculated binding affinities of TcdB to the 2 receptors, under pH 7.5 or pH 5, are labeled above each diagram. This measurement was calculated based on 2 biological replicates with standard deviations listed for each sample (raw data in ). (B) The structure comparisons of the TcdB-CRD2 complex at pH 7.5 and the 2 states at pH 5. (C) The helices (α2 and α4) of CRD2 that interact with TcdB are colored for each state. Dashed curves label the <t>CRD-binding</t> groove. Stars label the CRD-binding loop. Dark gray color labels regions in α-helices 2 and 4 that lack the cryo-EM density. The buried surface areas, calculated based on the model for the complex of TcdB and CRD2 under pH 7.5, state 1 and state 2 are around 700, 150, and 80 Å 2 , respectively. (D) The movement of the β-sheet (residues 1,812–1,827) in the D97 region are shown and color coded for each state. Tyr1819 of TcdB and its interaction partner Pro485 of CSPG4 are shown. (E) The same region rotated 90° from Panel D. BLI, bio-layer interferometry; CRD, cysteine-rich domain; CRD2, cysteine-rich domain <t>of</t> <t>frizzled-2;</t> TcdB, Toxin B.
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    Image Search Results


    (A) Binding kinetics between TcdB and receptors are measured by BLI. The calculated binding affinities of TcdB to the 2 receptors, under pH 7.5 or pH 5, are labeled above each diagram. This measurement was calculated based on 2 biological replicates with standard deviations listed for each sample (raw data in ). (B) The structure comparisons of the TcdB-CRD2 complex at pH 7.5 and the 2 states at pH 5. (C) The helices (α2 and α4) of CRD2 that interact with TcdB are colored for each state. Dashed curves label the CRD-binding groove. Stars label the CRD-binding loop. Dark gray color labels regions in α-helices 2 and 4 that lack the cryo-EM density. The buried surface areas, calculated based on the model for the complex of TcdB and CRD2 under pH 7.5, state 1 and state 2 are around 700, 150, and 80 Å 2 , respectively. (D) The movement of the β-sheet (residues 1,812–1,827) in the D97 region are shown and color coded for each state. Tyr1819 of TcdB and its interaction partner Pro485 of CSPG4 are shown. (E) The same region rotated 90° from Panel D. BLI, bio-layer interferometry; CRD, cysteine-rich domain; CRD2, cysteine-rich domain of frizzled-2; TcdB, Toxin B.

    Journal: PLoS Biology

    Article Title: Structural dynamics of receptor recognition and pH-induced dissociation of full-length Clostridioides difficile Toxin B

    doi: 10.1371/journal.pbio.3001589

    Figure Lengend Snippet: (A) Binding kinetics between TcdB and receptors are measured by BLI. The calculated binding affinities of TcdB to the 2 receptors, under pH 7.5 or pH 5, are labeled above each diagram. This measurement was calculated based on 2 biological replicates with standard deviations listed for each sample (raw data in ). (B) The structure comparisons of the TcdB-CRD2 complex at pH 7.5 and the 2 states at pH 5. (C) The helices (α2 and α4) of CRD2 that interact with TcdB are colored for each state. Dashed curves label the CRD-binding groove. Stars label the CRD-binding loop. Dark gray color labels regions in α-helices 2 and 4 that lack the cryo-EM density. The buried surface areas, calculated based on the model for the complex of TcdB and CRD2 under pH 7.5, state 1 and state 2 are around 700, 150, and 80 Å 2 , respectively. (D) The movement of the β-sheet (residues 1,812–1,827) in the D97 region are shown and color coded for each state. Tyr1819 of TcdB and its interaction partner Pro485 of CSPG4 are shown. (E) The same region rotated 90° from Panel D. BLI, bio-layer interferometry; CRD, cysteine-rich domain; CRD2, cysteine-rich domain of frizzled-2; TcdB, Toxin B.

    Article Snippet: The purified TcdB (0.3 mg/mL) was preincubated with FZD2-CRD-Fc (R&D Systems, Minneapolis, MN) in a 50-mM PBS buffer at 1:1 ratio under room temperature and pH 7.5 prior to the pH change.

    Techniques: Binding Assay, Labeling, Cryo-EM Sample Prep

    (A) TcdB (shown as a ribbon model) binds to the receptors (gray cartoon), CSPG4 and FZD2, before endosomal acidification. The proposed pore-forming helices of TcdB are shown as orange ribbon models. (B) TcdB dissociates from the receptors and the pore-forming helices rearrange. Gray arrows indicate the dissociation of TcdB. Orange arrows suggest the insertion of pore-forming helices into the endosomal membrane. CSPG4, chondroitin sulfate proteoglycan 4; FZD2, frizzled-2; TcdB, Toxin B.

    Journal: PLoS Biology

    Article Title: Structural dynamics of receptor recognition and pH-induced dissociation of full-length Clostridioides difficile Toxin B

    doi: 10.1371/journal.pbio.3001589

    Figure Lengend Snippet: (A) TcdB (shown as a ribbon model) binds to the receptors (gray cartoon), CSPG4 and FZD2, before endosomal acidification. The proposed pore-forming helices of TcdB are shown as orange ribbon models. (B) TcdB dissociates from the receptors and the pore-forming helices rearrange. Gray arrows indicate the dissociation of TcdB. Orange arrows suggest the insertion of pore-forming helices into the endosomal membrane. CSPG4, chondroitin sulfate proteoglycan 4; FZD2, frizzled-2; TcdB, Toxin B.

    Article Snippet: The purified TcdB (0.3 mg/mL) was preincubated with FZD2-CRD-Fc (R&D Systems, Minneapolis, MN) in a 50-mM PBS buffer at 1:1 ratio under room temperature and pH 7.5 prior to the pH change.

    Techniques: Membrane