title: Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus.
abstract: An acidic phospholipase A(2) was purified from Deinagkistrodon acutus (Agkistrodon acutus) which displays an inhibitory effect on platelet aggregation. The three-dimensional structure of the enzyme was determined by molecular replacement at 2.6 A resolution with a crystallographic R factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two molecules in the asymmetric unit form a dimer and the dimer formation accompanies a significant conformational adaptation of segment 14-23, a constituent of the 'interface recognition site' (IRS). This probably reflects the inherent structural flexibility of the IRS. The possible expansion of the site for inhibiting platelet aggregation as proposed previously [Wang et al. (1996), J. Mol. Biol. 255, 669-676] is discussed.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
authors.forename: Lichuan
authors.initials: L
authors.lastname: Gu
authors.forename: Hailong
authors.initials: H
authors.lastname: Zhang
authors.forename: Shiying
authors.initials: S
authors.lastname: Song
authors.forename: Yuancong
authors.initials: Y
authors.lastname: Zhou
authors.forename: Zhengjiong
authors.initials: Z
authors.lastname: Lin
mesh_terms: D017836:Agkistrodon; D000818:Animals; D003435:Crotalid Venoms / Q000201:enzymology*; D018360:Crystallography, X-Ray; D016297:Mutagenesis, Site-Directed; D010741:Phospholipases A / Q000737:chemistry* / Q000235:genetics; D054467:Phospholipases A2; D011487:Protein Conformation
chemical_list: D003435:Crotalid Venoms; D010741:Phospholipases A; D054467:Phospholipases A2