1ik8
From Proteopedia
(New page: 200px<br /><applet load="1ik8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ik8" /> '''NMR structure of Alpha-Bungarotoxin'''<br />...) |
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| - | [[Image:1ik8.jpg|left|200px]]<br /><applet load="1ik8" size=" | + | [[Image:1ik8.jpg|left|200px]]<br /><applet load="1ik8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ik8" /> | caption="1ik8" /> | ||
'''NMR structure of Alpha-Bungarotoxin'''<br /> | '''NMR structure of Alpha-Bungarotoxin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A combinatorial library approach was used to produce synthetic peptides | + | A combinatorial library approach was used to produce synthetic peptides mimicking the snake neurotoxin binding site of nicotinic receptors. Among the sequences, which inhibited binding of alpha-bungarotoxin to muscle and neuronal nicotinic receptors, HRYYESSLPWYPD, a 14-amino acid peptide with considerably higher toxin-binding affinity than the other synthesized peptides, was selected, and the structure of its complex with the toxin was analyzed by NMR. Comparison of the solution structure of the free toxin and its complex with this peptide indicated that complex formation induced extensive conformational rearrangements mainly at finger II and the carboxy terminus of the protein. The peptidyl residues P10 and Y4 seemed to be critical for peptide folding and complex stability, respectively. The latter residue of the peptide strongly interacted with the protein by entering a small pocket delimited by D30, C33, S34, R36, and V39 toxin side chains. |
==About this Structure== | ==About this Structure== | ||
| - | 1IK8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http:// | + | 1IK8 is a [http://en.wikipedia.org/wiki/Single_protein 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=1IK8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:42 2008'' |
Revision as of 11:12, 21 February 2008
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NMR structure of Alpha-Bungarotoxin
Overview
A combinatorial library approach was used to produce synthetic peptides mimicking the snake neurotoxin binding site of nicotinic receptors. Among the sequences, which inhibited binding of alpha-bungarotoxin to muscle and neuronal nicotinic receptors, HRYYESSLPWYPD, a 14-amino acid peptide with considerably higher toxin-binding affinity than the other synthesized peptides, was selected, and the structure of its complex with the toxin was analyzed by NMR. Comparison of the solution structure of the free toxin and its complex with this peptide indicated that complex formation induced extensive conformational rearrangements mainly at finger II and the carboxy terminus of the protein. The peptidyl residues P10 and Y4 seemed to be critical for peptide folding and complex stability, respectively. The latter residue of the peptide strongly interacted with the protein by entering a small pocket delimited by D30, C33, S34, R36, and V39 toxin side chains.
About this Structure
1IK8 is a Single protein structure of sequence from Bungarus multicinctus. Full crystallographic information is available from OCA.
Reference
NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor., Scarselli M, Spiga O, Ciutti A, Bernini A, Bracci L, Lelli B, Lozzi L, Calamandrei D, Di Maro D, Klein S, Niccolai N, Biochemistry. 2002 Feb 5;41(5):1457-63. PMID:11814338
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