Direct analysis of cooperativity in multisubunit allosteric proteins.

ABSTRACT: Allosteric regulation of protein function is a fundamental phenomenon of major importance in many cellular processes. Such regulation is often achieved by ligand-induced conformational changes in multimeric proteins that may give rise to cooperativity in protein function. At the heart of allosteric mechanisms offered to account for such phenomenon, involving either concerted or sequential conformational transitions, lie changes in intersubunit interactions along the ligation pathway of the protein. However, structure-function analysis of such homooligomeric proteins by means of mutagenesis, although it provides valuable indirect information regarding (allosteric) mechanisms of action, it does not define the contribution of individual subunits nor interactions thereof to cooperativity in pr

SUBMITTER: Zandany N 

PROVIDER: S-EPMC2575317 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature