2c9a
From Proteopedia
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CRYSTAL STRUCTURE OF THE MAM-IG MODULE OF RECEPTOR PROTEIN TYROSINE PHOSPHATASE MU
Overview
Type IIB receptor protein tyrosine phosphatases (RPTPs) are bi-functional, cell surface molecules. Their ectodomains mediate stable, homophilic, cell-adhesive interactions, whereas the intracellular catalytic regions, can modulate the phosphorylation state of cadherin/catenin complexes. We, describe a systematic investigation of the cell-adhesive properties of the, extracellular region of RPTPmu, a prototypical type IIB RPTP. The crystal, structure of a construct comprising its N-terminal MAM (meprin/A5/mu) and, Ig domains was determined at 2.7 A resolution; this assigns the MAM fold, to the jelly-roll family and reveals extensive interactions between the, two domains, which form a rigid structural unit. Structure-based, site-directed mutagenesis, serial domain deletions and ... [(full description)]
About this Structure
2C9A is a [Single protein] structure of sequence from [Homo sapiens] with NAG and NA as [ligands]. Active as [[1]], with EC number [3.1.3.48]. Full crystallographic information is available from [OCA].
Reference
Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion., Aricescu AR, Hon WC, Siebold C, Lu W, van der Merwe PA, Jones EY, EMBO J. 2006 Feb 22;25(4):701-12. Epub 2006 Feb 2. PMID:16456543
Page seeded by OCA on Mon Oct 29 20:06:36 2007
Categories: Homo sapiens | Single protein | Aricescu, A.R. | Hon, W.C. | Jones, E.Y. | Lu, W. | Merwe, P.A.Van.Der. | Siebold, C. | NA | NAG | Glycoprotein | Hydrolase | Immunoglobulin domain | Receptor
