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J. Biol. Chem., Vol. 266, Issue 32, 21530-21536, Nov, 1991
C Betzel, G Lange, GP Pal, KS Wilson, A Maelicke and W Saenger
The crystal structure of the "long" alpha-neurotoxin alpha-cobratoxin was
refined to an R-factor of 19.5% using 3271 x-ray data to 2.4-A resolution.
The polypeptide chain forms three loops, I, II, III, knotted together by
four disulfide bridges, with the most prominent, loop II, containing
another disulfide close to its lower tip. Loop I is stabilized by one
beta-turn and two beta-sheet hydrogen bonds; loop II by eight beta-sheet
hydrogen bonds, with the tip folded into two distorted right-handed helical
turns stabilized by two alpha-helical and two beta-turn hydrogen bonds; and
loop III by hydrophobic interactions and one beta-turn. Loop II and one
strand of loop III form an antiparallel triple-pleated beta-sheet, and
tight anchoring of the Asn63 side chain fixes the tail segment. In the
crystal lattice, the alpha-cobratoxin molecules dimerize by beta-sheet
formation between strands 53 and 57 of symmetry-related molecules. Because
such interactions are found also in a cardiotoxin and alpha-bungarotoxin,
this could be of importance for interaction with acetylcholine receptor.
The refined crystal structure of alpha-cobratoxin from Naja naja siamensis at 2.4-A resolution
European Molecular Biology Laboratory, Deutsches Elektronen Synchrotron, Hamburg, Federal Republic of Germany.
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