1rlw
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1RLW 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 CD and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1RLW 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 CD and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4]]. Structure known Active Sites: CA1, CA2, CR1, CR2 and CR3. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RLW OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2., Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL, J Biol Chem. 1998 Jan 16;273(3):1596-604. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9430701 9430701] | Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2., Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL, J Biol Chem. 1998 Jan 16;273(3):1596-604. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9430701 9430701] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Phospholipase A(2)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Perisic, O.]] | [[Category: Perisic, O.]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 10:44:01 2007'' |
Revision as of 08:39, 30 October 2007
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CALCIUM-PHOSPHOLIPID BINDING DOMAIN FROM CYTOSOLIC PHOSPHOLIPASE A2
Overview
Cytosolic phospholipase A2 (cPLA2) is a calcium-sensitive 85-kDa enzyme, that hydrolyzes arachidonic acid-containing membrane phospholipids to, initiate the biosynthesis of eicosanoids and platelet-activating factor, potent inflammatory mediators. The calcium-dependent activation of the, enzyme is mediated by an N-terminal C2 domain, which is responsible for, calcium-dependent translocation of the enzyme to membranes and that, enables the intact enzyme to hydrolyze membrane-resident substrates. The, 2.4-A x-ray crystal structure of this C2 domain was solved by multiple, isomorphous replacement and reveals a beta-sandwich with the same topology, as the C2 domain from phosphoinositide-specific phospholipase C delta 1., Two clusters of exposed hydrophobic residues surround two adjacent ... [(full description)]
About this Structure
1RLW is a [Single protein] structure of sequence from [Homo sapiens] with CD and CA as [ligands]. Active as [Phospholipase A(2)], with EC number [3.1.1.4]. Structure known Active Sites: CA1, CA2, CR1, CR2 and CR3. Full crystallographic information is available from [OCA].
Reference
Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2., Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL, J Biol Chem. 1998 Jan 16;273(3):1596-604. PMID:9430701
Page seeded by OCA on Tue Oct 30 10:44:01 2007
Categories: Homo sapiens | Phospholipase A(2) | Single protein | Perisic, O. | Williams, R.L. | CA | CD | C2 domain | Calb domain | Hydrolase
