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1rlw

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(New page: 200px<br /> <applet load="1rlw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rlw, resolution 2.4&Aring;" /> '''CALCIUM-PHOSPHOLIPID...)
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==About this Structure==
==About this Structure==
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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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RLW OCA]].
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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/Hydrolase Hydrolase]], 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==
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:43:57 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:44:43 2007''

Revision as of 06:40, 30 October 2007


1rlw, resolution 2.4Å

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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 [Hydrolase], 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

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