Structural highlights
Function
[PA2N_GLOHA] Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[1]
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 structure of agkistrodotoxin crystallized under basic conditions has been determined at 2.8 A resolution by the molecular-replacement technique and refined to a crystallographic R factor of 0.194 and a free R factor of 0.260 with good stereochemistry. The molecular packing in the crystal differs from other PLA(2)s. The six molecules in the asymmetric unit form three dimers linked by Ca(2+) ions in a near-perfect six-ligand octahedral coordinating system. Extensive intermolecular hydrophobic interactions occur at the interfacial recognition site of each neurotoxin molecule, which provides an insight into phospholipase A(2)-membrane interactions. This hydrophobic interaction-induced molecular association along the interfacial recognition site suggests a self-protection mechanism of agkistrodotoxin.
Structure of agkistrodotoxin in an orthorhombic crystal form with six molecules per asymmetric unit.,Tang L, Zhou YC, Lin ZJ Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):1986-96. PMID:10666574[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen YH, Wang YM, Hseu MJ, Tsai IH. Molecular evolution and structure-function relationships of crotoxin-like and asparagine-6-containing phospholipases A2 in pit viper venoms. Biochem J. 2004 Jul 1;381(Pt 1):25-34. PMID:15032748 doi:http://dx.doi.org/10.1042/BJ20040125
- ↑ Tang L, Zhou YC, Lin ZJ. Structure of agkistrodotoxin in an orthorhombic crystal form with six molecules per asymmetric unit. Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):1986-96. PMID:10666574
