1yfo: Difference between revisions
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==Overview== | ==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 . | 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== | ==About this Structure== | ||
1YFO is a | 1YFO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Structure known Active Sites: S1 and S2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YFO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:36:22 2007'' | ||
