- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1126/science.1079731
-
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- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2003
Journal article
Antibody multispecificity mediated by conformational diversity.
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