Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus.
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.
Gu
Lichuan
L
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Zhang
Hailong
H
Song
Shiying
S
Zhou
Yuancong
Y
Lin
Zhengjiong
Z
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
D003435:Crotalid Venoms; D010741:Phospholipases A; D054467:Phospholipases A2