2v5y

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spinqualitylabelsall models 2v5y, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU ECTODOMAIN

Overview

Cell-cell contacts are fundamental to multicellular organisms and are, subject to exquisite levels of control. Human RPTPmu is a type IIB, receptor protein tyrosine phosphatase that both forms an adhesive contact, itself and is involved in regulating adhesion by dephosphorylating, components of cadherin-catenin complexes. Here we describe a 3.1 angstrom, crystal structure of the RPTPmu ectodomain that forms a homophilic trans, (antiparallel) dimer with an extended and rigid architecture, matching the, dimensions of adherens junctions. Cell surface expression of deletion, constructs induces intercellular spacings that correlate with the, ectodomain length. These data suggest that the RPTPmu ectodomain acts as a, distance gauge and plays a key regulatory function, locking the, phosphatase ... [(full description)]

About this Structure

2V5Y is a [Single protein] structure of sequence from [Homo sapiens] with NAG and NA as [ligands]. Active as [Protein-tyrosine-phosphatase], with EC number [3.1.3.48]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism., Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ, van der Merwe PA, Jones EY, Science. 2007 Aug 31;317(5842):1217-20. PMID:17761881

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