1wch
From Proteopedia
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CRYSTAL STRUCTURE OF PTPL1 HUMAN TYROSINE PHOSPHATASE MUTATED IN COLORECTAL CANCER- EVIDENCE FOR A SECOND PHOSPHOTYROSINE SUBSTRATE RECOGNITION POCKET
Overview
Protein-tyrosine phosphatase-L1 (PTPL1, also known as FAP-1, PTP1E, PTP-BAS, and PTPN13) is mutated in a significant number of colorectal, tumors and may play a role in down-regulating signaling responses mediated, by phosphatidylinositol 3-kinase, although the precise substrates are as, yet unknown. In this study, we describe a 1.8 A resolution crystal, structure of a fully active fragment of PTPL1 encompassing the catalytic, domain. PTPL1 adopts the standard PTP fold, albeit with an unusually, positioned additional N-terminal helix, and shows an ordered phosphate in, the active site. Interestingly, a positively charged pocket is located, near the PTPL1 catalytic site, reminiscent of the second phosphotyrosine, binding site in PTP1B, which is required to dephosphorylate peptides, ... [(full description)]
About this Structure
1WCH is a [Single protein] structure of sequence from [Homo sapiens] with PO4 as [ligand]. Active as [Hydrolase], with EC number [3.1.3.48]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket., Villa F, Deak M, Bloomberg GB, Alessi DR, van Aalten DM, J Biol Chem. 2005 Mar 4;280(9):8180-7. Epub 2004 Dec 20. PMID:15611135
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