Binding induced conformational changes of proteins correlate with their intrinsic fluctuations: a case study of antibodies.

ABSTRACT:

Background

How antibodies recognize and bind to antigens can not be totally explained by rigid shape and electrostatic complimentarity models. Alternatively, pre-existing equilibrium hypothesis states that the native state of an antibody is not defined by a single rigid conformation but instead with an ensemble of similar conformations that co-exist at equilibrium. Antigens bind to one of the preferred conformations making this conformation more abundant shifting the equilibrium.

Results

Here, two antibodies, a germline antibody of 36-65 Fab and a monoclonal antibody, SPE7 are studied in detail to elucidate the mechanism of antibody-antigen recognition and to understand how a single antibody recognizes different antigens. An elastic network model, Anisotropic Network Model (

SUBMITTER: Keskin O 

PROVIDER: S-EPMC1888692 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature