1rpm

HUMAN RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU, DOMAIN 1

spinqualitylabelsall models 1rpm, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1rpm is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PTPRM_HUMAN Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Receptor-like protein-tyrosine phosphatases (RPTPs) play important roles in regulating intracellular processes. We have been investigating the regulation and function of RPTPmu, a receptor-like PTP related to the Ig superfamily of cell adhesion molecules. Recently, the crystal structure of a dimer of the membrane proximal domain of RPTPalpha (RPTPalpha D1) was described (Bilwes, A. M., den Hertog, J., Hunter, T., and Noel J. P. (1996) Nature 382, 555-559). Within this crystal structure, the catalytic site of each subunit of the dimer is sterically blocked by the insertion of the N-terminal helix-turn-helix segment of the dyad-related monomer. It was proposed that dimerization would lead to inhibition of catalytic activity and may provide a paradigm for the regulation of the RPTP family. We have determined the crystal structure, to 2.3 A resolution, of RPTPmu D1, which shares 46% sequence identity with that of RPTPalpha D1. Although the tertiary structures of RPTPalpha D1 and RPTPmu D1 are very similar, with a root mean square deviation between equivalent Calpha atoms of 1.1 A, the quaternary structures of these two proteins are different. Neither the catalytic site nor the N-terminal helix-turn-helix segment of RPTPmu D1 participates in protein-protein interactions. The catalytic site of RPTPmu D1 is unhindered and adopts an open conformation similar to that of the cytosolic PTP, PTP1B (Barford, D., Flint, A. J., and Tonks, N. K. (1994) Science 263, 1397-1404). We propose that dimerization-induced modulation of RPTP activity may not be a general feature of this family of enzymes. The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu.,Hoffmann KM, Tonks NK, Barford D J Biol Chem. 1997 Oct 31;272(44):27505-8. PMID:9346878 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosine phosphatase 3D structures

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