The crystal structure of human receptor protein tyrosine phosphatase ? phosphatase domain 1

Eswaran, Jeyanthy and Debreczeni, Judit E. and Longman, Emma and Barr, Alastair J. and Knapp, Stefan (2006) The crystal structure of human receptor protein tyrosine phosphatase ? phosphatase domain 1. Protein Science, 15 (6). pp. 1500-1505. ISSN 0961-8368

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Official URL: http://dx.doi.org/10.1110/ps.062128706

Abstract

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. RPTP? is a member of the R2A/IIb subfamily of RPTPs along with RPTP?, RPTP?, and RPTP?. Here, we have determined the crystal structure of catalytically active, monomeric D1 domain of RPTP? at 1.9 Å. Structural comparison with other PTP family members indicates an overall classical PTP architecture of twisted mixed ?-sheets flanked by ?-helices, in which the catalytically important WPD loop is in an unhindered open conformation. Though the residues forming the dimeric interface in the RPTP? structure are all conserved, they are not involved in the protein–protein interaction in RPTP?. The N-terminal ?-strand, formed by ?x association with ?y, is conserved only in RPTPs but not in cytosolic PTPs, and this feature is conserved in the RPTP? structure forming a ?-strand. Analytical ultracentrifugation studies show that the presence of reducing agents and higher ionic strength are necessary to maintain RPTP? as a monomer. In this family the crystal structure of catalytically active RPTP? D1 was solved as a dimer, but the dimerization was proposed to be a consequence of crystallization since the protein was monomeric in solution. In agreement, we show that RPTP? is monomeric in solution and crystal structure.

Item Type: Article
Subjects: University of Westminster > Science and Technology > Life Sciences, School of (No longer in use)
Depositing User: Rachel Wheelhouse
Date Deposited: 20 Jul 2012 14:17
Last Modified: 20 Jul 2012 14:17
URI: http://westminsterresearch.wmin.ac.uk/id/eprint/10873

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