View source for 1pqr


==Solution Conformation of alphaA-Conotoxin EIVA==
<StructureSection load='1pqr' size='340' side='right'caption='[[1pqr]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pqr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_ermineus Conus ermineus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1PQR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1pqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pqr OCA], [https://pdbe.org/1pqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pqr RCSB], [https://www.ebi.ac.uk/pdbsum/1pqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pqr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CA4A_CONER 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).
<div style="background-color:#fffaf0;">
== 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<ref>PMID:12900418</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pqr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Conus ermineus]]
[[Category: Large Structures]]
[[Category: Chi S-W]]
[[Category: Han K-H]]
[[Category: McIntosh JM]]
[[Category: Olivera BM]]
[[Category: Park K-H]]
[[Category: Suk J-E]]