1CJY

HUMAN CYTOSOLIC PHOSPHOLIPASE A2

Summary for 1CJY

• Entry DOI: 10.2210/pdb1cjy/pdb
• Descriptor: PROTEIN (CYTOSOLIC PHOSPHOLIPASE A2), CALCIUM ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: phospholipase, lipid-binding, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P47712
• Total number of polymer chains: 2
• Total formula weight: 171170.25

Authors

Dessen, A.,Tang, J.,Schmidt, H.,Stahl, M.,Clark, J.D.,Seehra, J.,Somers, W.S. (deposition date: 1999-04-20, release date: 2000-04-20, Last modification date: 2023-12-27)

Primary citation

Dessen, A.,Tang, J.,Schmidt, H.,Stahl, M.,Clark, J.D.,Seehra, J.,Somers, W.S.
Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism.
Cell(Cambridge,Mass.), 97:349-360, 1999

PubMed Abstract: 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.

PubMed: 10319815
DOI: 10.1016/S0092-8674(00)80744-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)