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Crystal structure of human dual specificity phosphatase, JNK stimulatory phosphatase-1, at 1.5 Å resolution

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Abstract

Human JNK stimulatory phosphatase-1 (JSP-1) is a novel member of dual specificity phosphatases. A C-terminus truncated JSP-1 was expressed in Escherichia coli and was crystallized using the sitting-drop vapor diffusion method. Thin-plate crystals obtained at 278 K belong to a monoclinic space group, C2, with unit-cell parameters a = 84.0 Å, b = 49.3 Å, c = 47.3 Å, and β = 119.5°, and diffract up to 1.5 Å resolution at 100 K. The structure of JSP-1 has a single compact (α/β) domain, which consists of six α-helices and five β-strands, and shows a conserved structural scaffold in regard to both DSPs and PTPs. A cleft formed by a PTP-loop at the active site is very shallow, and is occupied by one sulfonate compound, MES, at the bottom. In the binary complex structure of JSP-1 with MES, the conformations of three important segments in regard to the catalytic mechanism are not similar to those in PTP1B. JSP-1 has no loop corresponding to the Lys120-loop of PTP1B, and tryptophan residue corresponding to the substrate-stacking in PTP1B is substituted by alanine residue in JSP-1. Proteins 2007. © 2006 Wiley-Liss, Inc.

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