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| - | [[Image:1jln.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1jln.png|left|200px]] |
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| | {{STRUCTURE_1jln| PDB=1jln | SCENE= }} | | {{STRUCTURE_1jln| PDB=1jln | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11493009}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11493009 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11493009}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ptp-sl]] | | [[Category: Ptp-sl]] |
| | [[Category: Ptpbr7]] | | [[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 Tue Jul 1 20:26:11 2008'' |
Revision as of 17:26, 1 July 2008
Template:STRUCTURE 1jln
Crystal structure of the catalytic domain of protein tyrosine phosphatase PTP-SL/BR7
Template:ABSTRACT PUBMED 11493009
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 Tue Jul 1 20:26:11 2008
