1vhr
From Proteopedia
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[[Category: protein dual-specificity phosphatase]] | [[Category: protein dual-specificity phosphatase]] | ||
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Revision as of 17:37, 12 November 2007
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HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE
Overview
Dual specificity protein phosphatases (DSPs) regulate mitogenic signal, transduction and control the cell cycle. Here, the crystal structure of a, human DSP, vaccinia H1-related phosphatase (or VHR), was determined at 2.1, angstrom resolution. A shallow active site pocket in VHR allows for the, hydrolysis of phosphorylated serine, threonine, or tyrosine protein, residues, whereas the deeper active site of protein tyrosine phosphatases, (PTPs) restricts substrate specificity to only phosphotyrosine. Positively, charged crevices near the active site may explain the enzyme's preference, for substrates with two phosphorylated residues. The VHR structure defines, a conserved structural scaffold for both DSPs and PTPs. A "recognition, region," connecting helix alpha1 to strand beta1, may determine, differences in substrate specificity between VHR, the PTPs, and other, DSPs.
About this Structure
1VHR is a Single protein structure of sequence from Homo sapiens with SO4 and EPE as ligands. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Structure known Active Sites: GAA, GAB, PLA, PLB, RCA, RCB, VRA and VRB. Full crystallographic information is available from OCA.
Reference
Crystal structure of the dual specificity protein phosphatase VHR., Yuvaniyama J, Denu JM, Dixon JE, Saper MA, Science. 1996 May 31;272(5266):1328-31. PMID:8650541
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