1cjy
From Proteopedia
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HUMAN CYTOSOLIC PHOSPHOLIPASE A2
Overview
Cytosolic phospholipase A2 initiates the biosynthesis of prostaglandins, leukotrienes, and platelet-activating factor (PAF), mediators of the pathophysiology of asthma and arthritis. Here, we report the X-ray crystal structure of human cPLA2 at 2.5 A. cPLA2 consists of an N-terminal calcium-dependent lipid-binding/C2 domain and a catalytic unit whose topology is distinct from that of other lipases. An unusual Ser-Asp dyad located in a deep cleft at the center of a predominantly hydrophobic funnel selectively cleaves arachidonyl phospholipids. The structure reveals a flexible lid that must move to allow substrate access to the active site, thus explaining the interfacial activation of this important lipase.
About this Structure
1CJY is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism., Dessen A, Tang J, Schmidt H, Stahl M, Clark JD, Seehra J, Somers WS, Cell. 1999 Apr 30;97(3):349-60. PMID:10319815
Page seeded by OCA on Thu Feb 21 12:06:50 2008
Categories: Homo sapiens | Phospholipase A(2) | Single protein | Clark, J D. | Dessen, A. | Schmidt, H. | Seehra, J. | Somers, W S. | Stahl, M. | Tang, J. | CA | MES | Hydrolase | Lipid-binding | Phospholipase
