1fyr
From Proteopedia
DIMER FORMATION THROUGH DOMAIN SWAPPING IN THE CRYSTAL STRUCTURE OF THE GRB2-SH2 AC-PYVNV COMPLEX
Overview
Src homology 2 (SH2) domains are key modules in intracellular signal transduction. They link activated cell surface receptors to downstream targets by binding to phosphotyrosine-containing sequence motifs. The crystal structure of a Grb2-SH2 domain-phosphopeptide complex was determined at 2.4 A resolution. The asymmetric unit contains four polypeptide chains. There is an unexpected domain swap so that individual chains do not adopt a closed SH2 fold. Instead, reorganization of the EF loop leads to an open, nonglobular fold, which associates with an equivalent partner to generate an intertwined dimer. As in previously reported crystal structures of canonical Grb2-SH2 domain-peptide complexes, each of the four hybrid SH2 domains in the two domain-swapped dimers binds the phosphopeptide in a type I beta-turn conformation. This report is the first to describe domain swapping for an SH2 domain. While in vivo evidence of dimerization of Grb2 exists, our SH2 dimer is metastable and a physiological role of this new form of dimer formation remains to be demonstrated.
About this Structure
1FYR is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Dimer formation through domain swapping in the crystal structure of the Grb2-SH2-Ac-pYVNV complex., Schiering N, Casale E, Caccia P, Giordano P, Battistini C, Biochemistry. 2000 Nov 7;39(44):13376-82. PMID:11063574 Page seeded by OCA on Fri May 2 16:54:59 2008
