1yfo
From Proteopedia
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RECEPTOR PROTEIN TYROSINE PHOSPHATASE ALPHA, DOMAIN 1 FROM MOUSE
Overview
Receptor-like protein-tyrosine phosphatases (RPTPs), like their, non-receptor counterparts, regulate the level of, phosphotyrosine-containing proteins derived from the action of, protein-tyrosine kinases. RPTPs are type-I integral membrane proteins, which contain one or two catalytic domains in their cytoplasmic region. It, is not known whether extracellular ligands regulate the activity of RPTPs., Here we describe the crystal structure of the membrane-proximal catalytic, domain (D1) of a typical RPTP, murine RPTP alpha. Significant structural, deviations from the PTP1B fold reside within the amino-terminal, helix-turn-helix segment of RPTPalphaD1 (residues 214 to 242) and a, distinctive two-stranded beta-sheet formed between residues 211-213 and, 458-461. The turn of the N-terminal segment inserts into the active site, of a dyad-related D1 monomer. On the basis of two independent crystal, structures, sequence alignments, and the reported biological activity of, EGF receptor/CD45 chimaeras, we propose that dimerization and active-site, blockage is a physiologically important mechanism for downregulating the, catalytic activity of RPTPalpha and other RPTPs.
About this Structure
1YFO is a Single protein structure of sequence from Mus musculus. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization., Bilwes AM, den Hertog J, Hunter T, Noel JP, Nature. 1996 Aug 8;382(6591):555-9. PMID:8700232
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