1lar
From Proteopedia
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CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR
Contents |
Overview
Most receptor-like protein tyrosine phosphatases (RPTPs) contain two, conserved phosphatase domains (D1 and D2) in their intracellular region., The carboxy-terminal D2 domain has little or no catalytic activity. The, crystal structure of the tandem D1 and D2 domains of the human RPTP LAR, revealed that the tertiary structures of the LAR D1 and D2 domains are, very similar to each other, with the exception of conformational, differences at two amino acid positions in the D2 domain. Site-directed, mutational changes at these positions (Leu-1644-to-Tyr and, Glu-1779-to-Asp) conferred a robust PTPase activity to the D2 domain. The, catalytic sites of both domains are accessible, in contrast to the dimeric, blocked orientation model previously suggested. The relative orientation, of the LAR D1 and D2 domains, constrained by a short linker, is stabilized, by extensive interdomain interactions, suggesting that this orientation, might be favored in solution.
Disease
Known disease associated with this structure: Leukemia, acute myeloid OMIM:[604763]
About this Structure
1LAR is a Single protein structure of sequence from Homo sapiens. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Crystal structure of the tandem phosphatase domains of RPTP LAR., Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA, Cell. 1999 May 14;97(4):449-57. PMID:10338209
Page seeded by OCA on Mon Nov 12 17:58:14 2007
