This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1wch
From Proteopedia
|
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
Page seeded by OCA on Tue Oct 30 08:26:01 2007
