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Abstract

Analysis of x-ray crystal structures has clarified the nature of antibody-antigen interactions, and the conformational basis of specificity and affinity, but does not provide a clear picture of the dynamics of antigen recognition. In particular, we know that primary antibodies can bind a wider variety of ligands than their secondary counterparts-which are tuned for high specificity and affinity. Crystal structures show that in the absence of antigen the secondary antibody adopts a structure preformed for binding, but that the primary antibody does not. Our calculations show that the unligated state of the primary antibody has a well-defined structure, fluctuating no more widely than that of the secondary antibody, and undergoes a discrete structural rearrangement in response to ligand.

Original languageEnglish (US)
Article number208106
JournalPhysical Review Letters
Volume95
Issue number20
DOIs
Publication statusPublished - Nov 11 2005

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All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)

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