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1wch
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1WCH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with PO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1WCH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with PO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WCH OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15611135 15611135] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15611135 15611135] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aalten, D.M.F.Van.]] | [[Category: Aalten, D.M.F.Van.]] | ||
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[[Category: tyrosine phosphatase]] | [[Category: tyrosine phosphatase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:19:18 2007'' |
Revision as of 08:14, 30 October 2007
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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 [Protein-tyrosine-phosphatase], 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 10:19:18 2007
Categories: Homo sapiens | Protein-tyrosine-phosphatase | Single protein | Aalten, D.M.F.Van. | Alessi, D.R. | Bloomberg, G.B. | Deak, M. | Villa, F. | PO4 | Coiled coil | Colorectal cancer alternative splicing | Cytoskeleton | Hydrolase | Phosphate ion | Polymorphism | Structural protein | Tyrosine phosphatase
