1imi
From Proteopedia
(New page: 200px<br /><applet load="1imi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1imi" /> '''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1'''...) |
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| - | [[Image:1imi.gif|left|200px]]<br /><applet load="1imi" size=" | + | [[Image:1imi.gif|left|200px]]<br /><applet load="1imi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1imi" /> | caption="1imi" /> | ||
'''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1'''<br /> | '''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A 600 MHz NMR study of alpha-conotoxin ImI from Conus imperialis, targeting the alpha7 neuronal nicotinic acetylcholine receptor (nAChR), is | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1IMI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_imperialis Conus imperialis] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1IMI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_imperialis Conus imperialis] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Conus imperialis]] | [[Category: Conus imperialis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arseniev, A | + | [[Category: Arseniev, A S.]] |
| - | [[Category: Ivanov, V | + | [[Category: Ivanov, V T.]] |
| - | [[Category: Maslennikov, I | + | [[Category: Maslennikov, I V.]] |
| - | [[Category: Shenkarev, Z | + | [[Category: Shenkarev, Z O.]] |
| - | [[Category: Tsetlin, V | + | [[Category: Tsetlin, V I.]] |
| - | [[Category: Zhmak, M | + | [[Category: Zhmak, M N.]] |
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: acetylcholine receptor inhibitor]] | [[Category: acetylcholine receptor inhibitor]] | ||
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[[Category: postsynaptic]] | [[Category: postsynaptic]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:20 2008'' |
Revision as of 11:13, 21 February 2008
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SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1
Overview
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.
About this Structure
1IMI is a Single protein structure of sequence from Conus imperialis with as ligand. Full crystallographic information is available from OCA.
Reference
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
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