Tyrosine phosphorylation as a conformational switch: a case study of integrin β3 cytoplasmic tail.

ABSTRACT: Reversible protein phosphorylation is vital for many fundamental cellular processes. The actual impact of adding and removing phosphate group(s) is 3-fold: changes in the local/global geometry, alterations in the electrostatic potential and, as the result of both, modified protein-target interactions. Here we present a comprehensive structural investigation of the effects of phosphorylation on the conformational as well as functional states of a crucial cell surface receptor, α(IIb)β(3) integrin. We have analyzed phosphorylated (Tyr(747) and Tyr(759)) β(3) integrin cytoplasmic tail (CT) primarily by NMR, and our data demonstrate that under both aqueous and membrane-mimetic conditions, phosphorylation causes substantial conformational rearrangements. These changes originate from novel ionic

SUBMITTER: Deshmukh L 

PROVIDER: S-EPMC3220520 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature