Structural highlights
Function
[PA24A_HUMAN] Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dessen A, Tang J, Schmidt H, Stahl M, Clark JD, Seehra J, Somers WS. Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism. Cell. 1999 Apr 30;97(3):349-60. PMID:10319815
