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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism.

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.[1]

References

  1. Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism. Dessen, A., Tang, J., Schmidt, H., Stahl, M., Clark, J.D., Seehra, J., Somers, W.S. Cell (1999) [Pubmed]
 
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