Long-range cooperative binding effects in a T cell receptor variable domain.

ABSTRACT: Although cellular processes depend on protein-protein interactions, our understanding of molecular recognition between proteins remains far from comprehensive. Protein-protein interfaces are structural and energetic mosaics in which a subset of interfacial residues, called hot spots, contributes disproportionately to the affinity of the complex. These hot-spot residues can be further clustered into hot regions. It has been proposed that binding energetics between residues within a hot region are cooperative, whereas those between hot regions are strictly additive. If this idea held true for all protein-protein interactions, then energetically significant long-range conformational effects would be unlikely to occur. In the present study, we show cooperative binding energetics between distin

SUBMITTER: Moza B 

PROVIDER: S-EPMC1502545 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature