2gwo
From Proteopedia
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crystal structure of TMDP
Overview
The testis- and skeletal-muscle-specific dual-specificity phosphatase, (TMDP) is a member of the dual-specificity phosphatase (DSP) subgroup of, protein tyrosine phosphatases. TMDP has similar activities toward both, tyrosine and threonine phosphorylated substrates, and is supposed to be, involved in spermatogenesis. Here, we report the crystal structure of, human TMDP at a resolution of 2.4 A. In spite of high sequence similarity, with other DSPs, the crystal structure of TMDP shows distinct structural, motifs and surface properties. In TMDP, the alpha1-beta1 loop, a substrate, recognition motif is located further away from the active site loop in, comparison to prototype DSP Vaccinia H1 related phophatase (VHR), which, preferentially dephosphorylates tyrosine phosphorylated substrates and, down-regulates MAP kinase signaling. Residues in the active site residues, of TMDP are smaller in size and more hydrophobic than those of VHR. In, addition, TMDP cannot be aligned with VHR in loop beta3-alpha4. These, differences in the active site of TMDP result in a flat and wide pocket, structure, allowing equal binding of phosphotyrosine and phosphothreonine, substrates.
About this Structure
2GWO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity., Kim SJ, Jeong DG, Yoon TS, Son JH, Cho SK, Ryu SE, Kim JH, Proteins. 2007 Jan 1;66(1):239-45. PMID:17044055
Page seeded by OCA on Mon Nov 12 22:23:30 2007
