1rlw
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CALCIUM-PHOSPHOLIPID BINDING DOMAIN FROM CYTOSOLIC PHOSPHOLIPASE A2
OverviewOverview
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 StructureAbout 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].
ReferenceReference
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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