1kc4
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1kc4 |SIZE=350|CAPTION= <scene name='initialview01'>1kc4</scene> | |PDB= 1kc4 |SIZE=350|CAPTION= <scene name='initialview01'>1kc4</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=HSL:HOMOSERINE+LACTONE'>HSL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1abt|1ABT]], [[1idh|1IDH]], [[2abx|2ABX]], [[1i9b|1I9B]], [[1haj|1HAJ]], [[1hc9|1HC9]], [[1bxp|1BXP]], [[1jbd|1JBD]], [[1ikc|1IKC]], [[1kfh|1KFH]], [[1kl8|1KL8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kc4 OCA], [http://www.ebi.ac.uk/pdbsum/1kc4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kc4 RCSB]</span> | ||
}} | }} | ||
| Line 35: | Line 38: | ||
[[Category: protein-protein interaction]] | [[Category: protein-protein interaction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:46:22 2008'' |
Revision as of 18:46, 30 March 2008
| |||||||
| Ligands: | |||||||
| Related: | 1ABT, 1IDH, 2ABX, 1I9B, 1HAJ, 1HC9, 1BXP, 1JBD, 1IKC, 1KFH, 1KL8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR Structural Analysis of the Complex Formed Between alpha-Bungarotoxin and the Principal alpha-Neurotoxin Binding Sequence on the alpha7 Subunit of a Neuronal Nicotinic Acetylcholine Receptor
Overview
We report a new, higher resolution NMR structure of alpha-bungarotoxin that defines the structure-determining disulfide core and beta-sheet regions. We further report the NMR structure of the stoichiometric complex formed between alpha-bungarotoxin and a recombinantly expressed 19-mer peptide ((178)IPGKRTESFYECCKEPYPD(196)) derived from the alpha7 subunit of the chick neuronal nicotinic acetylcholine receptor. A comparison of these two structures reveals binding-induced stabilization of the flexible tip of finger II in alpha-bungarotoxin. The conformational rearrangements in the toxin create an extensive binding surface involving both sides of the alpha7 19-mer hairpin-like structure. At the contact zone, Ala(7), Ser(9), and Ile(11) in finger I and Arg(36), Lys(38), Val(39), and Val(40) in finger II of alpha-bungarotoxin interface with Phe(186), Tyr(187), Glu(188), and Tyr(194) in the alpha7 19-mer underscoring the importance of receptor aromatic residues as critical neurotoxin-binding determinants. Superimposing the structure of the complex onto that of the acetylcholine-binding protein (1I9B), a soluble homologue of the extracellular domain of the alpha7 receptor, places alpha-bungarotoxin at the peripheral surface of the inter-subunit interface occluding the agonist-binding site. The disulfide-rich core of alpha-bungarotoxin is suggested to be tilted in the direction of the membrane surface with finger II extending into the proposed ligand-binding cavity.
About this Structure
1KC4 is a Protein complex structure of sequences from Bungarus multicinctus and Gallus gallus. Full crystallographic information is available from OCA.
Reference
NMR structural analysis of alpha-bungarotoxin and its complex with the principal alpha-neurotoxin-binding sequence on the alpha 7 subunit of a neuronal nicotinic acetylcholine receptor., Moise L, Piserchio A, Basus VJ, Hawrot E, J Biol Chem. 2002 Apr 5;277(14):12406-17. Epub 2002 Jan 14. PMID:11790782
Page seeded by OCA on Sun Mar 30 21:46:22 2008
Categories: Bungarus multicinctus | Gallus gallus | Protein complex | Basus, V J. | Hawrot, E. | Moise, L. | Piserchio, A. | Alpha-bungarotoxin | Alpha-neurotoxin | Ligand-gated ion channel | Nicotinic acetylcholine receptor alpha 7 subunit | Nmr | Protein-peptide complex | Protein-protein interaction
