1cjy

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[[Image:1cjy.gif|left|200px]]
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{{STRUCTURE_1cjy| PDB=1cjy | SCENE= }}
{{STRUCTURE_1cjy| PDB=1cjy | SCENE= }}
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'''HUMAN CYTOSOLIC PHOSPHOLIPASE A2'''
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===HUMAN CYTOSOLIC PHOSPHOLIPASE A2===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10319815}}
==About this Structure==
==About this Structure==
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[[Category: Lipid-binding]]
[[Category: Lipid-binding]]
[[Category: Phospholipase]]
[[Category: Phospholipase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:51:08 2008''

Revision as of 17:51, 30 June 2008

Template:STRUCTURE 1cjy

HUMAN CYTOSOLIC PHOSPHOLIPASE A2

Template:ABSTRACT PUBMED 10319815

About this Structure

1CJY is a Single protein structure of sequence from Homo sapiens. 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

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