Membranes serve as allosteric activators of phospholipase a2, enabling it to extract, bind, and hydrolyze phospholipid substrates

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 6, 2015, Pages E516-E525

  Mouchlis, Varnavas D ^a   Bucher, Denis ^a   McCammon, J Andrew ^a,b   Dennis, Edward A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

DXMS; GIVA cPLA2; GVIA iPLA2; MD simulations; PAPC

Indexed keywords

CALCIUM INDEPENDENT PHOSPHOLIPASE A2; CYTOSOLIC PHOSPHOLIPASE A2; PHOSPHOLIPASE A2; PHOSPHOLIPID; PROTEIN BINDING;

ALLOSTERISM; ARTICLE; BILAYER MEMBRANE; CONFORMATIONAL TRANSITION; DEUTERIUM HYDROGEN EXCHANGE; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; EXTRACTION; LIGAND BINDING; LIPID HYDROLYSIS; MASS SPECTROMETRY; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; SIMULATION; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; HYDROLYSIS; MEMBRANE; METABOLISM; PHYSIOLOGY; X RAY CRYSTALLOGRAPHY;

ALLOSTERIC REGULATION; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROLYSIS; MEMBRANES; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PHOSPHOLIPASES A2; PHOSPHOLIPIDS; PROTEIN BINDING;

EID: 84922604138     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1424651112     Document Type: Article

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