Structural insights into the recognition of β3 integrin cytoplasmic tail by the SH3 domain of Src kinase.

ABSTRACT: Src kinase plays an important role in integrin signaling by regulating cytoskeletal organization and cell remodeling. Previous in vivo studies have revealed that the SH3 domain of c-Src kinase directly associates with the C-terminus of β3 integrin cytoplasmic tail. Here, we explore this binding interface with a combination of different spectroscopic and computational methods. Chemical shift mapping, PRE, transferred NOE and CD data were used to obtain a docked model of the complex. This model suggests a different binding mode from the one proposed through previous studies wherein, the C-terminal end of β3 spans the region in between the RT and n-Src loops of SH3 domain. Furthermore, we show that tyrosine phosphorylation of β3 prevents this interaction, supporting the notion of a constituti

SUBMITTER: Katyal P 

PROVIDER: S-EPMC3795494 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature