Summary
PDB 1CJY deposited: 1999-04-20 modified: 2009-02-24
Title HUMAN CYTOSOLIC PHOSPHOLIPASE A2
Authors Clark, J.D., Dessen, A., Schmidt, H., Seehra, J., Somers, W.S., Stahl, M., Tang, J.
Method X-RAY DIFFRACTION
Structure factors resolution 2.5 rfactor 0.229 rfree 0.298
DPI 0.79 theoretical min: 0.42
Citations

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.

Cell(Cambridge,Mass.) 1999 Apr; 97(3):349-360 doi:10.1016/S0092-8674(00)80744-8

Cross References
Database source Identifier Description
PubMed 10319815 CELLB5
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1CJY/1 1CJY 1 monomer 0 1 3 4092
1CJY/2 1CJY 2 monomer 0 1 3 3870