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Cited by 719

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Antibody Multispecificity Mediated by Conformational Diversity

James, Leo C., Roversi, Pietro, Tawfik, Dan S.·2003·Science

Abstract

A single antibody was shown to adopt different binding-site conformations and thereby bind unrelated antigens. Analysis by both x-ray crystallography and pre–steady-state kinetics revealed an equilibrium between different preexisting isomers, one of which possessed a promiscuous, low-affinity binding site for aromatic ligands, including the immunizing hapten. A subsequent induced-fit isomerization led to high-affinity complexes with a deep and narrow binding site. A protein antigen identified by repertoire selection made use of an unrelated antibody isomer with a wide, shallow binding site. Conformational diversity, whereby one sequence adopts multiple structures and multiple functions, can increase the effective size of the antibody repertoire but may also lead to autoimmunity and allergy.

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Crossref · 10.1126/science.1079731

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Metadata

Authors
James, L. C., Roversi, P., & Tawfik, D. S.
Venue
Science
Published
2003-02-28
Volume
299
Issue
5611
Pages
1362-1367
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1964126053
Cited by
719
References
1
FWCI
37.51
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Antibody Multispecificity Mediated by Conformational Diversity. https://app.cochat.ai/papers/10.1126/science.1079731
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James, L. C., Roversi, P., & Tawfik, D. S. (2003). Antibody Multispecificity Mediated by Conformational Diversity. Science. https://doi.org/10.1126/science.1079731

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.