1idh: Difference between revisions

Revision as of 10:48, 1 July 2008

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File:1idh.png

Template:STRUCTURE 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

Template:ABSTRACT PUBMED 11312275

About this StructureAbout this Structure

1IDH is a Protein complex structure of sequences from Bungarus multicinctus and Torpedo californica. Full experimental information is available from OCA.

ReferenceReference

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

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-[[Image:1idh.gif|left|200px]]
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 {{STRUCTURE_1idh|  PDB=1idh  |  SCENE=  }}
-'''THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE'''
+===THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE===
-==Overview==
+<!--
-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 line below this paragraph, {{ABSTRACT_PUBMED_11312275}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11312275 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11312275}}
 ==About this Structure==
-IDH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDH OCA].
+IDH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDH OCA].
 ==Reference==
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 [[Category: Nmr]]
 [[Category: Protein-protein interaction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:52:38 2008''
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