2abx
From Proteopedia
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THE CRYSTAL STRUCTURE OF ALPHA-BUNGAROTOXIN AT 2.5 ANGSTROMS RESOLUTION. RELATION TO SOLUTION STRUCTURE AND BINDING TO ACETYLCHOLINE RECEPTOR
Overview
We report collection of 2.5 A resolution X-ray diffraction data from newly, grown crystals of the rare 'small unit cell' form of the long snake, neurotoxin, alpha-bungarotoxin. The previous model of the molecule has, been rebuilt, and refined using least-square methods to a crystallographic, residual of 0.24 at 2.5 A resolution. alpha-Bungarotoxin's crystal, structure is compared with the crystal structures of two other snake, neurotoxins (cobratoxin and erabutoxin), and with its solution structure, inferred from spectroscopic studies. Significant differences include less, beta-sheet in bungarotoxin's crystal structure than in solution, or in the, crystal structures of other neurotoxins, and an unusual orientation in the, crystal of the invariant tryptophan. The functional, binding surface of, bungarotoxin is described; it consists primarily of hydrophobic and, hydrogen-bonding groups and only a few charged side-chains. The structure, is compared with experimental binding parameters for neurotoxins.
About this Structure
2ABX is a Single protein structure of sequence from Bungarus multicinctus. This structure superseeds the now removed PDB entry 1ABX. Full crystallographic information is available from OCA.
Reference
The crystal structure of alpha-bungarotoxin at 2.5 A resolution: relation to solution structure and binding to acetylcholine receptor., Love RA, Stroud RM, Protein Eng. 1986 Oct-Nov;1(1):37-46. PMID:3507686
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