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1lxh

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[[Image:1lxh.gif|left|200px]]
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{{STRUCTURE_1lxh| PDB=1lxh | SCENE= }}
{{STRUCTURE_1lxh| PDB=1lxh | SCENE= }}
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'''Solution structure of alpha-cobratoxin complexed with a cognate peptide (minimized average structure)'''
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===Solution structure of alpha-cobratoxin complexed with a cognate peptide (minimized average structure)===
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==Overview==
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The alpha18-mer peptide, spanning residues 181-198 of the Torpedo nicotinic acetylcholine receptor alpha1 subunit, contains key binding determinants for agonists and competitive antagonists. To investigate whether the alpha18-mer can bind other alpha-neurotoxins besides alpha-bungarotoxin, we designed a two-dimensional (1)H-(15)N heteronuclear single quantum correlation experiment to screen four related neurotoxins for their binding ability to the peptide. Of the four toxins tested (erabutoxin a, erabutoxin b, LSIII, and alpha-cobratoxin), only alpha-cobratoxin binds the alpha18-mer to form a 1:1 complex. The NMR solution structure of the alpha-cobratoxin.alpha18-mer complex was determined with a backbone root mean square deviation of 1.46 A. In the structure, alpha-cobratoxin contacts the alpha18-mer at the tips of loop I and II and through C-terminal cationic residues. The contact zone derived from the intermolecular nuclear Overhauser effects is in agreement with recent biochemical data. Furthermore, the structural models support the involvement of cation-pi interactions in stabilizing the complex. In addition, the binding screen results suggest that C-terminal cationic residues of alpha-bungarotoxin and alpha-cobratoxin contribute significantly to binding of the alpha18-mer. Finally, we present a structural model for nicotinic acetylcholine receptor-alpha-cobratoxin interaction by superimposing the alpha-cobratoxin.alpha18-mer complex onto the crystal structure of the acetylcholine-binding protein (Protein Data Bank code ).
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The line below this paragraph, {{ABSTRACT_PUBMED_12133834}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12133834 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12133834}}
==About this Structure==
==About this Structure==
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1LXH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Naja_kaouthia Naja kaouthia] 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=1LXH OCA].
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1LXH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Naja_kaouthia Naja kaouthia] 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=1LXH OCA].
==Reference==
==Reference==
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[[Category: Protein-protein interaction]]
[[Category: Protein-protein interaction]]
[[Category: Toxin,alpha-cobratoxin]]
[[Category: Toxin,alpha-cobratoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:23:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:46:09 2008''

Revision as of 19:46, 2 July 2008

Image:1lxh.png

Template:STRUCTURE 1lxh

Solution structure of alpha-cobratoxin complexed with a cognate peptide (minimized average structure)

Template:ABSTRACT PUBMED 12133834

About this Structure

1LXH is a Protein complex structure of sequences from Naja kaouthia and Torpedo californica. Full experimental information is available from OCA.

Reference

NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica., Zeng H, Hawrot E, J Biol Chem. 2002 Oct 4;277(40):37439-45. Epub 2002 Jul 19. PMID:12133834

Page seeded by OCA on Wed Jul 2 22:46:09 2008

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