Structural highlights
Function
[3S1EC_LATSE] Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Binds to Torpedo marmorata nAChR (Kd=0.14 nM) (PubMed:7721859).[1]
Publication Abstract from PubMed
Erabutoxin-b, M(r) = 6861.1, a single 62 amino-acid chain folded by four disulfide bridges, was crystallized in a new orthorhombic form by using thiocyanate as crystallizing agent. The space group is P2(1)2(1)2(1) with a = 53.36 (4), b = 40.89 (4), c = 55.71 (5) A, V = 121533.1 A and Z = 8. X-ray diffraction data were recorded at the LURE synchrotron facility (lambda = 1.405 A). The structure was solved by molecular replacement and shows a dimeric association through an anti-parallel beta-sheet around the twofold non-crystallographic axis. The two independent molecules, one SCN- ion and 97 associated water molecules were refined by molecular dynamics and annealing techniques to R = 19.6% (10,913 Fobs, resolution 5-1.7 A). The thiocyanate ion is located at the interface of the dimer and close to the non-crystallographic twofold axis.
Structure determination of a dimeric form of erabutoxin-b, crystallized from a thiocyanate solution.,Saludjian P, Prange T, Navaza J, Menez R, Guilloteau JP, Ries-Kautt M, Ducruix A Acta Crystallogr B. 1992 Aug 1;48 ( Pt 4):520-31. PMID:1418823[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tremeau O, Lemaire C, Drevet P, Pinkasfeld S, Ducancel F, Boulain JC, Menez A. Genetic engineering of snake toxins. The functional site of Erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues. J Biol Chem. 1995 Apr 21;270(16):9362-9. PMID:7721859
- ↑ Saludjian P, Prange T, Navaza J, Menez R, Guilloteau JP, Ries-Kautt M, Ducruix A. Structure determination of a dimeric form of erabutoxin-b, crystallized from a thiocyanate solution. Acta Crystallogr B. 1992 Aug 1;48 ( Pt 4):520-31. PMID:1418823
