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| {{STRUCTURE_2gwo| PDB=2gwo | SCENE= }} | | {{STRUCTURE_2gwo| PDB=2gwo | SCENE= }} |
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| '''crystal structure of TMDP'''
| | ===crystal structure of TMDP=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_17044055}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17044055 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17044055}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ryu, S E.]] | | [[Category: Ryu, S E.]] |
| [[Category: Alpha/beta]] | | [[Category: Alpha/beta]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:37:43 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:30:48 2008'' |
