1lar
From Proteopedia
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| - | [[Image:1lar.gif|left|200px]] | + | [[Image:1lar.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR''' | + | {{Structure |
| + | |PDB= 1lar |SIZE=350|CAPTION= <scene name='initialview01'>1lar</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LAR is a [ | + | 1LAR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAR OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the tandem phosphatase domains of RPTP LAR., Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA, Cell. 1999 May 14;97(4):449-57. PMID:[http:// | + | Crystal structure of the tandem phosphatase domains of RPTP LAR., Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA, Cell. 1999 May 14;97(4):449-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10338209 10338209] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
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[[Category: tyrosine phosphatease]] | [[Category: tyrosine phosphatease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:40 2008'' |
Revision as of 10:28, 20 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR
Contents |
Overview
Most receptor-like protein tyrosine phosphatases (RPTPs) contain two conserved phosphatase domains (D1 and D2) in their intracellular region. The carboxy-terminal D2 domain has little or no catalytic activity. The crystal structure of the tandem D1 and D2 domains of the human RPTP LAR revealed that the tertiary structures of the LAR D1 and D2 domains are very similar to each other, with the exception of conformational differences at two amino acid positions in the D2 domain. Site-directed mutational changes at these positions (Leu-1644-to-Tyr and Glu-1779-to-Asp) conferred a robust PTPase activity to the D2 domain. The catalytic sites of both domains are accessible, in contrast to the dimeric blocked orientation model previously suggested. The relative orientation of the LAR D1 and D2 domains, constrained by a short linker, is stabilized by extensive interdomain interactions, suggesting that this orientation might be favored in solution.
Disease
Known disease associated with this structure: Leukemia, acute myeloid OMIM:[604763]
About this Structure
1LAR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the tandem phosphatase domains of RPTP LAR., Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA, Cell. 1999 May 14;97(4):449-57. PMID:10338209
Page seeded by OCA on Thu Mar 20 12:28:40 2008
