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1ien
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ieo|1ieo]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ieo|1ieo]]</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=1ien FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ien OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ien RCSB], [http://www.ebi.ac.uk/pdbsum/1ien 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=1ien FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ien OCA], [http://pdbe.org/1ien PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ien RCSB], [http://www.ebi.ac.uk/pdbsum/1ien PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 1ien" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:04, 11 September 2015
SOLUTION STRUCTURE OF TIA
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Categories: Adams, D A | Adams, D J | Alewood, P F | Atkins, A | Craik, D J | Gehrmann, J | Lewis, R J | Loughnan, M L | Palant, E | Sharpe, I A | Thomas, L | Alpha1-adrenoceptor | Conotoxin | Toxin
