2c7s
CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE KAPPA AT 1.95A RESOLUTION
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OverviewOverview
The receptor-type protein tyrosine phosphatases (RPTPs) are integral, membrane proteins composed of extracellular adhesion molecule-like, domains, a single transmembrane domain, and a cytoplasmic domain. The, cytoplasmic domain consists of tandem PTP domains, of which the D1 domain, is enzymatically active. RPTPkappa is a member of the R2A/IIb subfamily of, RPTPs along with RPTPmu, RPTPrho, and RPTPlambda. Here, we have determined, the crystal structure of catalytically active, monomeric D1 domain of, RPTPkappa at 1.9 A. Structural comparison with other PTP family members, indicates an overall classical PTP architecture of twisted mixed, beta-sheets flanked by alpha-helices, in which the catalytically important, WPD loop is in an unhindered open conformation. Though the residues, forming ... [(full description)]
About this StructureAbout this Structure
2C7S is a [Single protein] structure of sequence from [Homo sapiens] with ACT as [ligand]. Active as [[1]], with EC number [3.1.3.48]. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1., Eswaran J, Debreczeni JE, Longman E, Barr AJ, Knapp S, Protein Sci. 2006 Jun;15(6):1500-5. Epub 2006 May 2. PMID:16672235
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