1ul2
From Proteopedia
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| - | [[Image:1ul2.jpg|left|200px]] | + | [[Image:1ul2.jpg|left|200px]] |
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| - | '''Solution Conformation of alpha-Conotoxin GIC''' | + | {{Structure |
| + | |PDB= 1ul2 |SIZE=350|CAPTION= <scene name='initialview01'>1ul2</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution Conformation of alpha-Conotoxin GIC''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UL2 is a [ | + | 1UL2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UL2 OCA]. |
==Reference== | ==Reference== | ||
| - | Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem J. 2004 Jun 1;380(Pt 2):347-52. PMID:[http:// | + | Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem J. 2004 Jun 1;380(Pt 2):347-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14992691 14992691] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chi, S W.]] | [[Category: Chi, S W.]] | ||
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[[Category: beta-turn]] | [[Category: beta-turn]] | ||
[[Category: c-terminal amidation]] | [[Category: c-terminal amidation]] | ||
| - | [[Category: two disulfide | + | [[Category: two disulfide bond]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:33:21 2008'' |
Revision as of 12:33, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution Conformation of alpha-Conotoxin GIC
Overview
Alpha-conotoxin GIC is a 16-residue peptide isolated from the venom of the cone snail Conus geographus. Alpha-conotoxin GIC potently blocks the alpha3beta2 subtype of human nicotinic acetylcholine receptor, showing a high selectivity for neuronal versus muscle subtype [McIntosh, Dowell, Watkins, Garrett, Yoshikami, and Olivera (2002) J. Biol. Chem. 277, 33610-33615]. We have now determined the three-dimensional solution structure of alpha-conotoxin GIC by NMR spectroscopy. The structure of alpha-conotoxin GIC is well defined with backbone and heavy atom root mean square deviations (residues 2-16) of 0.53 A and 0.96 A respectively. Structure and surface comparison of alpha-conotoxin GIC with the other alpha4/7 subfamily conotoxins reveals unique structural aspects of alpha-conotoxin GIC. In particular, the structural comparison between alpha-conotoxins GIC and MII indicates molecular features that may confer their similar receptor specificity profile, as well as those that provide the unique binding characteristics of alpha-conotoxin GIC.
About this Structure
1UL2 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution conformation of alpha-conotoxin GIC, a novel potent antagonist of alpha3beta2 nicotinic acetylcholine receptors., Chi SW, Kim DH, Olivera BM, McIntosh JM, Han KH, Biochem J. 2004 Jun 1;380(Pt 2):347-52. PMID:14992691
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