1pqr
From Proteopedia
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- | [[Image:1pqr.jpg|left|200px]] | + | [[Image:1pqr.jpg|left|200px]] |
- | + | ||
- | '''Solution Conformation of alphaA-Conotoxin EIVA''' | + | {{Structure |
+ | |PDB= 1pqr |SIZE=350|CAPTION= <scene name='initialview01'>1pqr</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Solution Conformation of alphaA-Conotoxin EIVA''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1PQR is a [ | + | 1PQR 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=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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/12900418 12900418] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chi, S W.]] | [[Category: Chi, S W.]] | ||
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[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
[[Category: c-term amidation]] | [[Category: c-term 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 13:27:47 2008'' |
Revision as of 11:27, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
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]. 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
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