1ien: Difference between revisions

Latest revision as of 18:41, 29 November 2023

SOLUTION STRUCTURE OF TIA

Structural highlights

1ien is a 1 chain structure with sequence from Conus tulipa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:	NH2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4] ^[5]

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^[6]

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

References

↑ Sharpe IA, Gehrmann J, Loughnan ML, Thomas L, Adams DA, Atkins A, Palant E, Craik DJ, Adams DJ, Alewood PF, Lewis RJ. Two new classes of conopeptides inhibit the alpha1-adrenoceptor and noradrenaline transporter. Nat Neurosci. 2001 Sep;4(9):902-7. PMID:11528421 doi:https://dx.doi.org/10.1038/nn0901-902
↑ Sharpe IA, Thomas L, Loughnan M, Motin L, Palant E, Croker DE, Alewood D, Chen S, Graham RM, Alewood PF, Adams DJ, Lewis RJ. Allosteric alpha 1-adrenoreceptor antagonism by the conopeptide rho-TIA. J Biol Chem. 2003 Sep 5;278(36):34451-7. Epub 2003 Jun 24. PMID:12824165 doi:https://dx.doi.org/10.1074/jbc.M305410200
↑ Chen Z, Rogge G, Hague C, Alewood D, Colless B, Lewis RJ, Minneman KP. Subtype-selective noncompetitive or competitive inhibition of human alpha1-adrenergic receptors by rho-TIA. J Biol Chem. 2004 Aug 20;279(34):35326-33. Epub 2004 Jun 11. PMID:15194691 doi:https://dx.doi.org/10.1074/jbc.M403703200
↑ Lima V, Mueller A, Kamikihara SY, Raymundi V, Alewood D, Lewis RJ, Chen Z, Minneman KP, Pupo AS. Differential antagonism by conotoxin rho-TIA of contractions mediated by distinct alpha1-adrenoceptor subtypes in rat vas deferens, spleen and aorta. Eur J Pharmacol. 2005 Jan 31;508(1-3):183-92. Epub 2005 Jan 12. PMID:15680270 doi:https://dx.doi.org/10.1016/j.ejphar.2004.12.011
↑ Ragnarsson L, Wang CI, Andersson A, Fajarningsih D, Monks T, Brust A, Rosengren KJ, Lewis RJ. Conopeptide rho-TIA defines a new allosteric site on the extracellular surface of the alpha1B-adrenoceptor. J Biol Chem. 2013 Jan 18;288(3):1814-27. doi: 10.1074/jbc.M112.430785. Epub 2012 , Nov 26. PMID:23184947 doi:https://dx.doi.org/10.1074/jbc.M112.430785
↑ Sharpe IA, Gehrmann J, Loughnan ML, Thomas L, Adams DA, Atkins A, Palant E, Craik DJ, Adams DJ, Alewood PF, Lewis RJ. Two new classes of conopeptides inhibit the alpha1-adrenoceptor and noradrenaline transporter. Nat Neurosci. 2001 Sep;4(9):902-7. PMID:11528421 doi:https://dx.doi.org/10.1038/nn0901-902

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Sharpe IA, Gehrmann J, Loughnan ML, Thomas L, Adams DA, Atkins A, Palant E, Craik DJ, Adams DJ, Alewood PF, Lewis RJ. Two new classes of conopeptides inhibit the alpha1-adrenoceptor and noradrenaline transporter. Nat Neurosci. 2001 Sep;4(9):902-7. PMID:11528421 doi:https://dx.doi.org/10.1038/nn0901-902

[2] Sharpe IA, Thomas L, Loughnan M, Motin L, Palant E, Croker DE, Alewood D, Chen S, Graham RM, Alewood PF, Adams DJ, Lewis RJ. Allosteric alpha 1-adrenoreceptor antagonism by the conopeptide rho-TIA. J Biol Chem. 2003 Sep 5;278(36):34451-7. Epub 2003 Jun 24. PMID:12824165 doi:https://dx.doi.org/10.1074/jbc.M305410200

[3] Chen Z, Rogge G, Hague C, Alewood D, Colless B, Lewis RJ, Minneman KP. Subtype-selective noncompetitive or competitive inhibition of human alpha1-adrenergic receptors by rho-TIA. J Biol Chem. 2004 Aug 20;279(34):35326-33. Epub 2004 Jun 11. PMID:15194691 doi:https://dx.doi.org/10.1074/jbc.M403703200

[4] Lima V, Mueller A, Kamikihara SY, Raymundi V, Alewood D, Lewis RJ, Chen Z, Minneman KP, Pupo AS. Differential antagonism by conotoxin rho-TIA of contractions mediated by distinct alpha1-adrenoceptor subtypes in rat vas deferens, spleen and aorta. Eur J Pharmacol. 2005 Jan 31;508(1-3):183-92. Epub 2005 Jan 12. PMID:15680270 doi:https://dx.doi.org/10.1016/j.ejphar.2004.12.011

[5] Ragnarsson L, Wang CI, Andersson A, Fajarningsih D, Monks T, Brust A, Rosengren KJ, Lewis RJ. Conopeptide rho-TIA defines a new allosteric site on the extracellular surface of the alpha1B-adrenoceptor. J Biol Chem. 2013 Jan 18;288(3):1814-27. doi: 10.1074/jbc.M112.430785. Epub 2012 , Nov 26. PMID:23184947 doi:https://dx.doi.org/10.1074/jbc.M112.430785

[6] Sharpe IA, Gehrmann J, Loughnan ML, Thomas L, Adams DA, Atkins A, Palant E, Craik DJ, Adams DJ, Alewood PF, Lewis RJ. Two new classes of conopeptides inhibit the alpha1-adrenoceptor and noradrenaline transporter. Nat Neurosci. 2001 Sep;4(9):902-7. PMID:11528421 doi:https://dx.doi.org/10.1038/nn0901-902

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[5]

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@@ Line 1: / Line 1: @@
 ==SOLUTION STRUCTURE OF TIA==
-<StructureSection load='1ien' size='340' side='right'caption='[[1ien]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1ien' size='340' side='right'caption='[[1ien]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ien]] is a 1 chain structure. 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>
+<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='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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ieo|1ieo]]</div></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>
+[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 ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Conus tulipa]]
 [[Category: Large Structures]]
-[[Category: Adams, D A]]
+[[Category: Adams DA]]
-[[Category: Adams, D J]]
+[[Category: Adams DJ]]
-[[Category: Alewood, P F]]
+[[Category: Alewood PF]]
-[[Category: Atkins, A]]
+[[Category: Atkins A]]
-[[Category: Craik, D J]]
+[[Category: Craik DJ]]
-[[Category: Gehrmann, J]]
+[[Category: Gehrmann J]]
-[[Category: Lewis, R J]]
+[[Category: Lewis RJ]]
-[[Category: Loughnan, M L]]
+[[Category: Loughnan ML]]
-[[Category: Palant, E]]
+[[Category: Palant E]]
-[[Category: Sharpe, I A]]
+[[Category: Sharpe IA]]
-[[Category: Thomas, L]]
+[[Category: Thomas L]]
-[[Category: Alpha1-adrenoceptor]]
-[[Category: Conotoxin]]
-[[Category: Toxin]]

1ien: Difference between revisions

Latest revision as of 18:41, 29 November 2023

SOLUTION STRUCTURE OF TIA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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