1jln
From Proteopedia
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[[Image:1jln.gif|left|200px]] | [[Image:1jln.gif|left|200px]] | ||
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'''Crystal structure of the catalytic domain of protein tyrosine phosphatase PTP-SL/BR7''' | '''Crystal structure of the catalytic domain of protein tyrosine phosphatase PTP-SL/BR7''' | ||
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[[Category: Scheidig, A J.]] | [[Category: Scheidig, A J.]] | ||
[[Category: Szedlacsek, S E.]] | [[Category: Szedlacsek, S E.]] | ||
| - | [[Category: | + | [[Category: Erk2-map kinase regulation]] |
| - | [[Category: | + | [[Category: Protein tyrosine phosphatase]] |
| - | [[Category: | + | [[Category: Ptp-sl]] |
| - | [[Category: | + | [[Category: Ptpbr7]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:22:30 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:22, 2 May 2008
Crystal structure of the catalytic domain of protein tyrosine phosphatase PTP-SL/BR7
Overview
Protein tyrosine phosphatases PTP-SL and PTPBR7 are isoforms belonging to cytosolic membrane-associated and to receptor-like PTPs (RPTPs), respectively. They represent a new family of PTPs with a major role in activation and translocation of MAP kinases. Specifically, the complex formation between PTP-SL and ERK2 involves an unusual interaction leading to the phosphorylation of PTP-SL by ERK2 at Thr253 and the inactivating dephosphorylation of ERK2 by PTP-SL. This interaction is strictly dependent upon a kinase interaction motif (KIM) (residues 224-239) situated at the N terminus of the PTP-SL catalytic domain. We report the first crystal structure of the catalytic domain for a member of this family (PTP-SL, residues 254-549, identical with residues 361-656 of PTPBR7), providing an example of an RPTP with single cytoplasmic domain, which is monomeric, having an unhindered catalytic site. In addition to the characteristic PTP-core structure, PTP-SL has an N-terminal helix, possibly orienting the KIM motif upon interaction with the target ERK2. An unusual residue in the catalytically important WPD loop promotes formation of a hydrophobically and electrostatically stabilised clamp. This could induce increased rigidity to the WPD loop and therefore reduced catalytic activity, in agreement with our kinetic measurements. A docking model based on the PTP-SL structure suggests that, in the complex with ERK2, the phosphorylation of PTP-SL should be accomplished first. The subsequent dephosphorylation of ERK2 seems to be possible only if a conformational rearrangement of the two interacting partners takes place.
About this Structure
1JLN is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation., Szedlacsek SE, Aricescu AR, Fulga TA, Renault L, Scheidig AJ, J Mol Biol. 2001 Aug 17;311(3):557-68. PMID:11493009 Page seeded by OCA on Fri May 2 21:22:30 2008
