1imi
From Proteopedia
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| - | [[Image:1imi.gif|left|200px]] | + | [[Image:1imi.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1''' | + | {{Structure |
| + | |PDB= 1imi |SIZE=350|CAPTION= <scene name='initialview01'>1imi</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IMI is a [ | + | 1IMI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Conus_imperialis Conus imperialis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10050774 10050774] |
[[Category: Conus imperialis]] | [[Category: Conus imperialis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: postsynaptic]] | [[Category: postsynaptic]] | ||
| - | ''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 11:52:15 2008'' |
Revision as of 09:52, 20 March 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. 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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