1vhr

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spinqualitylabelsall models 1vhr, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 ... [(full description)]

About this Structure

1VHR is a [Single protein] structure of sequence from [Homo sapiens] with SO4 and EPE as [ligands]. Active as [[1]], with EC number [3.1.3.48]. 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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