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1pqr
From Proteopedia
(New page: 200px<br /><applet load="1pqr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pqr" /> '''Solution Conformation of alphaA-Conotoxin EI...) |
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| - | [[Image:1pqr.jpg|left|200px]]<br /><applet load="1pqr" size=" | + | [[Image:1pqr.jpg|left|200px]]<br /><applet load="1pqr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pqr" /> | caption="1pqr" /> | ||
'''Solution Conformation of alphaA-Conotoxin EIVA'''<br /> | '''Solution Conformation of alphaA-Conotoxin EIVA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the solution three-dimensional structure of an alphaA-conotoxin | + | We report the solution three-dimensional structure of an alphaA-conotoxin EIVA determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. The alphaA-conotoxin EIVA consists of 30 amino acids representing the largest peptide among the alpha/alphaA-family conotoxins discovered so far and targets the neuromuscular nicotinic acetylcholine receptor with high affinity. alphaA-Conotoxin EIVA consists of three distinct structural domains. The first domain is mainly composed of the Cys3-Cys11-disulfide loop and is structurally ill-defined with a large backbone root mean square deviation of 1.91 A. The second domain formed by residues His12-Hyp21 is extremely well defined with a backbone root mean square deviation of 0.52 A, thus forming a sturdy stem for the entire molecule. The third C-terminal domain formed by residues Hyp22-Gly29 shows an intermediate structural order having a backbone root mean square deviation of 1.04 A. A structurally ill-defined N-terminal first loop domain connected to a rigid central molecular stem seems to be the general structural feature of the alphaA-conotoxin subfamily. A detailed structural comparison between alphaA-conotoxin EIVA and alphaA-conotoxin PIVA suggests that the higher receptor affinity of alphaA-conotoxin EIVA than alphaA-conotoxin PIVA might originate from different steric disposition and charge distribution in the second loop "handle" motif. |
==About this Structure== | ==About this Structure== | ||
| - | 1PQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] 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=1PQR OCA]. |
==Reference== | ==Reference== | ||
Solution conformation of alphaA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus., Chi SW, Park KH, Suk JE, Olivera BM, McIntosh JM, Han KH, J Biol Chem. 2003 Oct 24;278(43):42208-13. Epub 2003 Aug 4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12900418 12900418] | Solution conformation of alphaA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus., Chi SW, Park KH, Suk JE, Olivera BM, McIntosh JM, Han KH, J Biol Chem. 2003 Oct 24;278(43):42208-13. Epub 2003 Aug 4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12900418 12900418] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chi, S | + | [[Category: Chi, S W.]] |
| - | [[Category: Han, K | + | [[Category: Han, K H.]] |
| - | [[Category: McIntosh, J | + | [[Category: McIntosh, J M.]] |
| - | [[Category: Olivera, B | + | [[Category: Olivera, B M.]] |
| - | [[Category: Park, K | + | [[Category: Park, K H.]] |
| - | [[Category: Suk, J | + | [[Category: Suk, J E.]] |
[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
| Line 23: | Line 23: | ||
[[Category: two disulfide bonds]] | [[Category: two disulfide bonds]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:44 2008'' |
Revision as of 12:31, 21 February 2008
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Solution Conformation of alphaA-Conotoxin EIVA
Overview
We report the solution three-dimensional structure of an alphaA-conotoxin EIVA determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. The alphaA-conotoxin EIVA consists of 30 amino acids representing the largest peptide among the alpha/alphaA-family conotoxins discovered so far and targets the neuromuscular nicotinic acetylcholine receptor with high affinity. alphaA-Conotoxin EIVA consists of three distinct structural domains. The first domain is mainly composed of the Cys3-Cys11-disulfide loop and is structurally ill-defined with a large backbone root mean square deviation of 1.91 A. The second domain formed by residues His12-Hyp21 is extremely well defined with a backbone root mean square deviation of 0.52 A, thus forming a sturdy stem for the entire molecule. The third C-terminal domain formed by residues Hyp22-Gly29 shows an intermediate structural order having a backbone root mean square deviation of 1.04 A. A structurally ill-defined N-terminal first loop domain connected to a rigid central molecular stem seems to be the general structural feature of the alphaA-conotoxin subfamily. A detailed structural comparison between alphaA-conotoxin EIVA and alphaA-conotoxin PIVA suggests that the higher receptor affinity of alphaA-conotoxin EIVA than alphaA-conotoxin PIVA might originate from different steric disposition and charge distribution in the second loop "handle" motif.
About this Structure
1PQR is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
Solution conformation of alphaA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus., Chi SW, Park KH, Suk JE, Olivera BM, McIntosh JM, Han KH, J Biol Chem. 2003 Oct 24;278(43):42208-13. Epub 2003 Aug 4. PMID:12900418
Page seeded by OCA on Thu Feb 21 14:31:44 2008
