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1fpr
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(New page: 200px<br /> <applet load="1fpr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpr, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:49, 12 November 2007
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CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.
Overview
The substrate specificity of the catalytic domain of SHP-1, an important, regulator in the proliferation and development of hematopoietic cells, is, critical for understanding the physiological functions of SHP-1. Here we, report the crystal structures of the catalytic domain of SHP-1 complexed, with two peptide substrates derived from SIRPalpha, a member of the, signal-regulatory proteins. We show that the variable beta5-loop-beta6, motif confers SHP-1 substrate specificity at the P-4 and further, N-terminal subpockets. We also observe a novel residue shift at P-2, the, highly conserved subpocket in protein- tyrosine phosphatases. Our, observations provide new insight into the substrate specificity of SHP-1.
About this Structure
1FPR is a Single protein structure of sequence from Homo sapiens. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1., Yang J, Cheng Z, Niu T, Liang X, Zhao ZJ, Zhou GW, J Biol Chem. 2000 Feb 11;275(6):4066-71. PMID:10660565
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