1imi

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[[Image:1imi.png|left|200px]]
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==SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1==
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<StructureSection load='1imi' size='340' side='right' caption='[[1imi]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1imi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Conus_imperialis Conus imperialis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IMI FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1imi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1imi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1imi RCSB], [http://www.ebi.ac.uk/pdbsum/1imi PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A 600 MHz NMR study of alpha-conotoxin ImI from Conus imperialis, targeting the alpha7 neuronal nicotinic acetylcholine receptor (nAChR), is presented. ImI backbone spatial structure is well defined basing on the NOEs, spin-spin coupling constants, and amide protons hydrogen-deuterium exchange data: rmsd of the backbone atom coordinates at the 2-12 region is 0.28 A in the 20 best structures. The structure is described as a type I beta-turn (positions 2-5) followed by a distorted helix (positions 5-11). Similar structural patterns can be found in all neuronal-specific alpha-conotoxins. Highly mobile side chains of the Asp-5, Arg-7 and Trp-10 residues form a single site for ImI binding to the alpha7 receptor. When depicted with opposite directions of the polypeptide chains, the ImI helix and the tip of the central loop of long chain snake neurotoxins demonstrate a common scaffold and similar positioning of the functional side chains, both of these structural elements appearing essential for binding to the neuronal nAChRs.
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{{STRUCTURE_1imi| PDB=1imi | SCENE= }}
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NMR spatial structure of alpha-conotoxin ImI reveals a common scaffold in snail and snake toxins recognizing neuronal nicotinic acetylcholine receptors.,Maslennikov IV, Shenkarev ZO, Zhmak MN, Ivanov VT, Methfessel C, Tsetlin VI, Arseniev AS FEBS Lett. 1999 Feb 12;444(2-3):275-80. PMID:10050774<ref>PMID:10050774</ref>
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===SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_10050774}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1imi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Conus_imperialis Conus imperialis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMI OCA].
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</StructureSection>
[[Category: Conus imperialis]]
[[Category: Conus imperialis]]
[[Category: Arseniev, A S.]]
[[Category: Arseniev, A S.]]

Revision as of 11:29, 28 September 2014

SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1

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