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2iui

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(New page: 200px<br /> <applet load="2iui" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iui, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 20:41, 12 November 2007

Image:2iui.gif

2iui, resolution 2.40Å

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CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH PDGFR PHOSPHOTYROSYL PEPTIDE

Overview

Crystal structures of the amino-terminal SH2 domain of the p85alpha, subunit of phosphatidylinositol (PI) 3-kinase, alone and in complex with, phosphopeptides bearing pTyr-Met/Val-Xaa-Met motifs, show that, phosphopeptides bind in the two-pronged manner seen in high-affinity Lck, and Src SH2 complexes, with conserved interactions between the domain and, the peptide segment from phosphotyrosine to Met+3. Peptide binding, requires the rearrangement of a tyrosyl side chain in the BG loop to, create the hydrophobic Met+3 binding pocket. The structures suggest a, mechanism for the biological specificity exhibited by PI 3-kinase in its, interactions with phosphoprotein partners.

About this Structure

2IUI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes., Nolte RT, Eck MJ, Schlessinger J, Shoelson SE, Harrison SC, Nat Struct Biol. 1996 Apr;3(4):364-74. PMID:8599763

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