1mtq

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[[Image:1mtq.jpg|left|200px]]
[[Image:1mtq.jpg|left|200px]]
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{{Structure
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|PDB= 1mtq |SIZE=350|CAPTION= <scene name='initialview01'>1mtq</scene>
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The line below this paragraph, containing "STRUCTURE_1mtq", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>
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{{STRUCTURE_1mtq| PDB=1mtq | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mtq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mtq OCA], [http://www.ebi.ac.uk/pdbsum/1mtq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mtq RCSB]</span>
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'''THREE-DIMENSIONAL SOLUTION STRUCTURE OF ALPHA-CONOTOXIN GID BY NMR SPECTROSCOPY'''
'''THREE-DIMENSIONAL SOLUTION STRUCTURE OF ALPHA-CONOTOXIN GID BY NMR SPECTROSCOPY'''
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==About this Structure==
==About this Structure==
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1MTQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MTQ OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MTQ OCA].
==Reference==
==Reference==
Isolation, structure, and activity of GID, a novel alpha 4/7-conotoxin with an extended N-terminal sequence., Nicke A, Loughnan ML, Millard EL, Alewood PF, Adams DJ, Daly NL, Craik DJ, Lewis RJ, J Biol Chem. 2003 Jan 31;278(5):3137-44. Epub 2002 Nov 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12419800 12419800]
Isolation, structure, and activity of GID, a novel alpha 4/7-conotoxin with an extended N-terminal sequence., Nicke A, Loughnan ML, Millard EL, Alewood PF, Adams DJ, Daly NL, Craik DJ, Lewis RJ, J Biol Chem. 2003 Jan 31;278(5):3137-44. Epub 2002 Nov 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12419800 12419800]
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[[Category: Protein complex]]
 
[[Category: Adams, D J.]]
[[Category: Adams, D J.]]
[[Category: Alewood, P F.]]
[[Category: Alewood, P F.]]
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[[Category: Millard, E L.]]
[[Category: Millard, E L.]]
[[Category: Nicke, A.]]
[[Category: Nicke, A.]]
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[[Category: alpha-helix]]
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[[Category: Alpha-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:42:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:58 2008''
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Revision as of 22:42, 2 May 2008

Template:STRUCTURE 1mtq

THREE-DIMENSIONAL SOLUTION STRUCTURE OF ALPHA-CONOTOXIN GID BY NMR SPECTROSCOPY


Overview

Using assay-directed fractionation of Conus geographus crude venom, we isolated alpha-conotoxin GID, which acts selectively at neuronal nicotinic acetylcholine receptors (nAChRs). Unlike other neuronally selective alpha-conotoxins, alpha-GID has a four amino acid N-terminal tail, gamma-carboxyglutamate (Gla), and hydroxyproline (O) residues, and lacks an amidated C terminus. GID inhibits alpha 7 and alpha 3 beta 2 nAChRs with IC(50) values of 5 and 3 nm, respectively and is at least 1000-fold less potent at the alpha 1 beta 1 gamma delta, alpha 3 beta 4, and alpha 4 beta 4 combinations. GID also potently inhibits the alpha 4 beta 2 subtype (IC(50) of 150 nm). Deletion of the N-terminal sequence (GID Delta 1-4) significantly decreased activity at the alpha 4 beta 2 nAChR but hardly affected potency at alpha 3 beta 2 and alpha 7 nAChRs, despite enhancing the off-rates at these receptors. In contrast, Arg(12) contributed to alpha 4 beta 2 and alpha 7 activity but not to alpha 3 beta 2 activity. The three-dimensional structure of GID is well defined over residues 4-19 with a similar motif to other alpha-conotoxins. However, despite its influence on activity, the tail appears to be disordered in solution. Comparison of GID with other alpha 4/7-conotoxins which possess an NN(P/O) motif in loop II, revealed a correlation between increasing length of the aliphatic side-chain in position 10 (equivalent to 13 in GID) and greater alpha 7 versus alpha 3 beta 2 selectivity.

About this Structure

Full crystallographic information is available from OCA.

Reference

Isolation, structure, and activity of GID, a novel alpha 4/7-conotoxin with an extended N-terminal sequence., Nicke A, Loughnan ML, Millard EL, Alewood PF, Adams DJ, Daly NL, Craik DJ, Lewis RJ, J Biol Chem. 2003 Jan 31;278(5):3137-44. Epub 2002 Nov 4. PMID:12419800 Page seeded by OCA on Sat May 3 01:42:19 2008

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