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'''BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY''' | '''BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY''' | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10728829 10728829] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10728829 10728829] | ||
[[Category: Gloydius halys]] | [[Category: Gloydius halys]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lin, Z J.]] | [[Category: Lin, Z J.]] | ||
[[Category: Zhao, K H.]] | [[Category: Zhao, K H.]] | ||
[[Category: | [[Category: Agkistrodon halys palla]] | ||
[[Category: | [[Category: Anticoagulant activity]] | ||
[[Category: | [[Category: Basic phospholipase a2]] | ||
[[Category: | [[Category: Dimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:04:30 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 11:04, 2 May 2008
BASIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS-IMPLICATIONS FOR ITS ASSOCIATION AND ANTICOAGULANT ACTIVITIES BY X-RAY CRYSTALLOGRAPHY
OverviewOverview
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.
About this StructureAbout this Structure
1B4W is a Single protein structure of sequence from Gloydius halys. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Fri May 2 11:04:30 2008