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- | [[Image:1qs3.jpg|left|200px]] | + | {{Seed}} |
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| {{STRUCTURE_1qs3| PDB=1qs3 | SCENE= }} | | {{STRUCTURE_1qs3| PDB=1qs3 | SCENE= }} |
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- | '''NMR SOLUTION CONFORMATION OF AN ANTITOXIC ANALOG OF ALPHA-CONOTOXIN GI'''
| + | ===NMR SOLUTION CONFORMATION OF AN ANTITOXIC ANALOG OF ALPHA-CONOTOXIN GI=== |
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- | ==Overview==
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- | The three-dimensional solution conformation of an 11-residue antitoxic analogue of alpha-conotoxin GI, des-Glu1-[Cys3Ala]-des-Cys13-conotoxin GI (CANPACGRHYS-NH(2), designated "GI-15" henceforth), has been determined using two-dimensional (1)H NMR spectroscopy. The disulfide loop region (1C-6C) and the C-terminal tail (8R-11S) are connected by a flexible hinge formed near 7G, and the pairwise backbone rmsds for the former and the latter are 0.58 and 0.65 A, respectively. Superpositioning GI-15 with the structure of alpha-conotoxin GI shows that the two share an essentially identical fold in the common first disulfide loop region (1C-6C). However, the absence of the second disulfide loop in GI-15 results in segmental motion of the C-terminal half, causing the key receptor subtype selectivity residue 8R (Arg9 in alpha-conotoxin GI) to lose its native spatial orientation. The combined features of structural equivalence in the disulfide loop and a mobile C-terminal tail appear to be responsible for the activity of GI-15 as a competitive antagonist against native toxin. Electrostatic surface potential comparisons of the first disulfide region of GI-15 with other alpha-conotoxins or receptor-bound states of acetylcholine and d-tubocurarine show a common protruding surface that may serve as the minimal binding determinant for the neuromuscular acetylcholine receptor alpha 1-subunit. On the basis of the original "Conus toxin macrosite model" [Olivera, B. M., Rivier, J., Scott, J. K., Hillyard, D. R., and Cruz, L. J. (1991) J. Biol. Chem. 266, 1923-1936], we propose a revised binding model which incorporates these results. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10508392}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 10508392 is the PubMed ID number. |
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| + | {{ABSTRACT_PUBMED_10508392}} |
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| ==About this Structure== | | ==About this Structure== |
- | 1QS3 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QS3 OCA]. | + | 1QS3 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QS3 OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Conotoxin]] | | [[Category: Conotoxin]] |
| [[Category: Nicotinic acetylcholine receptor]] | | [[Category: Nicotinic acetylcholine receptor]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:38:30 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:50:44 2008'' |
Revision as of 18:50, 28 July 2008
Template:STRUCTURE 1qs3
NMR SOLUTION CONFORMATION OF AN ANTITOXIC ANALOG OF ALPHA-CONOTOXIN GI
Template:ABSTRACT PUBMED 10508392
About this Structure
1QS3 is a Single protein structure. Full experimental information is available from OCA.
Reference
NMR solution conformation of an antitoxic analogue of alpha-conotoxin GI: identification of a common nicotinic acetylcholine receptor alpha 1-subunit binding surface for small ligands and alpha-conotoxins., Mok KH, Han KH, Biochemistry. 1999 Sep 14;38(37):11895-904. PMID:10508392
Page seeded by OCA on Mon Jul 28 21:50:44 2008