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Antibody multispecificity mediated by conformational diversity.

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...

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Publication status:
Published

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Publisher copy:
10.1126/science.1079731

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
Role:
Author
Journal:
Science (New York, N.Y.)
Volume:
299
Issue:
5611
Pages:
1362-1367
Publication date:
2003-02-05
DOI:
EISSN:
1095-9203
ISSN:
0036-8075
URN:
uuid:acb3420d-be81-4661-8347-f24cd19640bd
Source identifiers:
23974
Local pid:
pubs:23974

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