Structural highlights
Function[PTPRF_HUMAN] Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase).[1] The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.[2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMost 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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