1b4w

BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY

spinqualitylabelsall models 1b4w, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1b4w is a 4 chain structure with sequence from Gloydius halys. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: BOG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PA2BB_GLOHA Snake venom phospholipase A2 (PLA2) that shows potent hemolytic activity, and exhibits medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 90 nM). It is one of the few phospholipases A2 capable of hydrolyzing the phospholipids of E.coli membranes in the presence of a bactericidal/permeability-increasing protein (BPI) of neutrophils. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The basic phospholipase A2 (PLA2) from the venom of Agkistrodon halys Pallas is a potent hemolytic toxin and anticoagulant. Crystal structure of the enzyme complexed with detergent n-octyl beta-D-glucopyranoside (beta-OG) in monoclinic crystal form has been determined to 2.6 A resolution. Beta-OG molecules were found in the hydrophobic channels of the enzyme. SDS-PAGE and dynamic light scattering measurements showed that the enzyme had a strong tendency to dimerise in aqueous solution. In the crystal structure the enzyme molecules associate into a tetramer with pseudo 222 symmetry, and the interfacial recognition site linked dimers constituting the tetramer have intensive interface interactions, and may be stable in solution. The structure reveals a unique positively charged face at the C-terminal region and a characteristic non-cationic 'anticoagulant' region (53-77). The face is supposed to be the hemolytic site, and based on sequence and structure comparison residues Trp70 and Glu53 instead of the basic residues in 'anticoagulant' region might play an important role in the anticoagulant activity. Structure of basic phospholipase A2 from Agkistrodon halys Pallas: implications for its association, hemolytic and anticoagulant activities.,Zhao K, Zhou Y, Lin Z Toxicon. 2000 Jul;38(7):901-16. PMID:10728829 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phospholipase A2 3D structures

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