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1pqr

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Revision as of 08:11, 24 February 2018

Solution Conformation of alphaA-Conotoxin EIVA

Structural highlights

1pqr is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CA4A_CONER] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin binds with high affinity to both fetal (alpha-1/beta-1/epsilon/delta subunits) and adult (alpha-1/beta-1/gamma/delta subunits) mammalian muscle nicotinic acetylcholine receptors (nAChR).

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chi SW, Park KH, Suk JE, Olivera BM, McIntosh JM, Han KH. Solution conformation of alphaA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus. J Biol Chem. 2003 Oct 24;278(43):42208-13. Epub 2003 Aug 4. PMID:12900418 doi:http://dx.doi.org/10.1074/jbc.M303342200

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pqr"

@@ Line 1: / Line 1: @@
 ==Solution Conformation of alphaA-Conotoxin EIVA==
 <StructureSection load='1pqr' size='340' side='right' caption='[[1pqr]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1pqr]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PQR FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pqr OCA], [http://pdbe.org/1pqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pqr RCSB], [http://www.ebi.ac.uk/pdbsum/1pqr PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pqr OCA], [http://pdbe.org/1pqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pqr RCSB], [http://www.ebi.ac.uk/pdbsum/1pqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pqr ProSAT]</span></td></tr>
 </table>
 == Function ==

1pqr

From Proteopedia

Revision as of 08:11, 24 February 2018

Solution Conformation of alphaA-Conotoxin EIVA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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