1kfh: Difference between revisions

Revision as of 10:15, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kfh.png

Template:STRUCTURE 1kfh

Solution Structure of alpha-Bungarotoxin by NMR SpectroscopySolution Structure of alpha-Bungarotoxin by NMR Spectroscopy

Template:ABSTRACT PUBMED 11790782

About this StructureAbout this Structure

1KFH is a Single protein structure of sequence from Bungarus multicinctus. Full experimental information is available from OCA.

ReferenceReference

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

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 {{STRUCTURE_1kfh|  PDB=1kfh  |  SCENE=  }}
-'''Solution Structure of alpha-Bungarotoxin by NMR Spectroscopy'''
+===Solution Structure of alpha-Bungarotoxin by NMR Spectroscopy===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11790782}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11790782 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11790782}}
 ==About this Structure==
-KFH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFH OCA].
+KFH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFH OCA].
 ==Reference==
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 [[Category: Alpha-bungarotoxin]]
 [[Category: Long snake neurotoxin]]
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