1idh

THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDETHE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE

Structural highlights 1idh is a 2 chain structure with sequence from Bungarus multicinctus and Pacific electric ray. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: Related: 1idg, 1idi, 1idl Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [NXL1A_BUNMU] Binds with high affinity to muscular and neuronal (alpha-7, alpha-8, and alpha-9) nicotinic acetylcholine receptors. Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Blocks the extracellular increase of dopamine evoked by nicotine only at the higher dose (4.2 uM). [ACHA_TORCA] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. 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 region encompassing residues 181-98 on the alpha1 subunit of the muscle-type nicotinic acetylcholine receptor forms a major determinant for the binding of alpha-neurotoxins. We have prepared an (15)N-enriched 18-amino acid peptide corresponding to the sequence in this region to facilitate structural elucidation by multidimensional NMR. Our aim was to determine the structural basis for the high affinity, stoichiometric complex formed between this cognate peptide and alpha-bungarotoxin, a long alpha-neurotoxin. Resonances in the complex were assigned through heteronuclear and homonuclear NMR experiments, and the resulting interproton distance constraints were used to generate ensemble structures of the complex. Thr(8), Pro(10), Lys(38), Val(39), Val(40), and Pro(69) in alpha-bungarotoxin and Tyr(189), Tyr(190), Thr(191), Cys(192), Asp(195), and Thr(196) in the peptide participate in major intermolecular contacts. A comparison of the free and bound alpha-bungarotoxin structures reveals significant conformational rearrangements in flexible regions of alpha-bungarotoxin, mainly loops I, II, and the C-terminal tail. Furthermore, several of the calculated structures suggest that cation-pi interactions may be involved in binding. The root mean square deviation of the polypeptide backbone in the complex is 2.07 A. This structure provides, to date, the highest resolution description of the contacts between a prototypic alpha-neurotoxin and its cognate recognition sequence. The solution structure of the complex formed between alpha-bungarotoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.,Zeng H, Moise L, Grant MA, Hawrot E J Biol Chem. 2001 Jun 22;276(25):22930-40. Epub 2001 Apr 18. PMID:11312275 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bungarotoxin

spinqualitylabelsall models 1idh, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image