1kba

CRYSTAL STRUCTURE OF KAPPA-BUNGAROTOXIN AT 2.3-ANGSTROM RESOLUTION

spinqualitylabelsall models 1kba, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1kba is a 2 chain structure with sequence from Bungarus multicinctus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 3LKB_BUNMU Postsynaptic neurotoxin that binds and inhibits neuronal nicotinic acetylcholine receptors (nAChR) with high affinity (IC(50)<100 nM). Is a selective, and slowly reversible antagonist of alpha-3/CHRNA3-containing and some alpha-4/CHRNA4-containing AChRs. 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 kappa-Neurotoxins display a very low affinity for neuromuscular receptors, but bind tightly to, and inhibit, nicotinic acetylcholine receptors in neuronal tissue such as the chick ciliary ganglia. In contrast, alpha-neurotoxins bind with high affinity and inhibit nicotinic acetylcholine receptors at the neuromuscular junction. The origin of this difference in specificity has been a long-studied question in the field. Here we report the first crystal structure of a kappa-neurotoxin, kappa-bungarotoxin. Unlike the NMR structure previously reported [Sutcliffe, M. J., Dobson, C. M., & Oswald, R. E. (1992) Biochemistry 31, 2962-2970], the present crystal structure more accurately defines the polypeptide fold and the nature of the interaction between subunits in the active dimer, which is a unique feature of the kappa-neurotoxins. The structure has been refined to R = 19.6% with X-ray diffraction data extending to a resolution of 2.3 A. There are two independent protein molecules (66 amino acid residues each) in the asymmetric unit that are arranged as a dimer with the two subunits related by a rotation of 178.6 degrees. Each subunit consists of three main-chain loops. Three of the five beta-strands of each subunit form an antiparallel beta-sheet which becomes an extended six-stranded antiparallel beta-sheet, by virtue of the approximate 2-fold symmetry of the dimer. The interactions at the dimer interface consist of six main-chain-main-chain hydrogen bonds, as well as three other hydrogen-bonding interactions involving side chains.(ABSTRACT TRUNCATED AT 250 WORDS) Crystal structure of kappa-bungarotoxin at 2.3-A resolution.,Dewan JC, Grant GA, Sacchettini JC Biochemistry. 1994 Nov 8;33(44):13147-54. PMID:7947721 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bungarotoxin 3D structures

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