View source for 1ien


==SOLUTION STRUCTURE OF TIA==
<StructureSection load='1ien' size='340' side='right'caption='[[1ien]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ien]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_tulipa Conus tulipa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IEN 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=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=1ien FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ien OCA], [https://pdbe.org/1ien PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ien RCSB], [https://www.ebi.ac.uk/pdbsum/1ien PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ien ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CA1A_CONTU CA1A_CONTU] Allosteric inhibitor of alpha-1B adrenergic receptors (ADRA1B). Binds to an allosteric modulatory site on transmembrane helix 6 and 7 at the base of extracellular loop 3 of ADRA1B (PubMed:23184947). Also weekly inhibits alpha-1A (ADRA1A) and alpha-1D (ADRA1D) adrenergic receptors in a competive manner (PubMed:15194691). Potently inhibits contractions of vas deferens, spleen and aorta in response to noradrenaline (PubMed:15680270).<ref>PMID:11528421</ref> <ref>PMID:12824165</ref> <ref>PMID:15194691</ref> <ref>PMID:15680270</ref> <ref>PMID:23184947</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cone snails use venom containing a cocktail of peptides ('conopeptides') to capture their prey. Many of these peptides also target mammalian receptors, often with exquisite selectivity. Here we report the discovery of two new classes of conopeptides. One class targets alpha1-adrenoceptors (rho-TIA from the fish-hunting Conus tulipa), and the second class targets the neuronal noradrenaline transporter (chi-MrIA and chi-MrIB from the mollusk-hunting C. marmoreus). rho-TIA and chi-MrIA selectively modulate these important membrane-bound proteins. Both peptides act as reversible non-competitive inhibitors and provide alternative avenues for the identification of inhibitor drugs.

Two new classes of conopeptides inhibit the alpha1-adrenoceptor and noradrenaline transporter.,Sharpe IA, Gehrmann J, Loughnan ML, Thomas L, Adams DA, Atkins A, Palant E, Craik DJ, Adams DJ, Alewood PF, Lewis RJ Nat Neurosci. 2001 Sep;4(9):902-7. PMID:11528421<ref>PMID:11528421</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ien" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Conus tulipa]]
[[Category: Large Structures]]
[[Category: Adams DA]]
[[Category: Adams DJ]]
[[Category: Alewood PF]]
[[Category: Atkins A]]
[[Category: Craik DJ]]
[[Category: Gehrmann J]]
[[Category: Lewis RJ]]
[[Category: Loughnan ML]]
[[Category: Palant E]]
[[Category: Sharpe IA]]
[[Category: Thomas L]]