7ofg
From Proteopedia
(Difference between revisions)
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<StructureSection load='7ofg' size='340' side='right'caption='[[7ofg]]' scene=''> | <StructureSection load='7ofg' size='340' side='right'caption='[[7ofg]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[7ofg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OFG FirstGlance]. <br> |
| - | </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=7ofg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ofg OCA], [https://pdbe.org/7ofg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ofg RCSB], [https://www.ebi.ac.uk/pdbsum/7ofg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ofg ProSAT]</span></td></tr> | + | </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=7ofg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ofg OCA], [https://pdbe.org/7ofg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ofg RCSB], [https://www.ebi.ac.uk/pdbsum/7ofg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ofg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NEU1_HUMAN NEU1_HUMAN] Neurophysin 1 specifically binds oxytocin. Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. Acts by binding to oxytocin receptor (OXTR) (PubMed:18174156).<ref>PMID:18174156</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Oxytocin is a neuropeptide that binds copper ions in nature. The structure of oxytocin in interaction with Cu(2+) was determined here by NMR, showing which atoms of the peptide are involved in binding. Paramagnetic relaxation enhancement NMR analyses indicated a binding mechanism where the amino terminus was required for binding and subsequently Tyr2, Ile3 and Gln4 bound in that order. The aromatic ring of Tyr2 formed a pi-cation interaction with Cu(2+). Oxytocin copper complex structure revealed by paramagnetic relaxation enhancement NMR analyses. | ||
| + | |||
| + | Determining the structure and binding mechanism of oxytocin-Cu(2+) complex using paramagnetic relaxation enhancement NMR analysis.,Alshanski I, Shalev DE, Yitzchaik S, Hurevich M J Biol Inorg Chem. 2021 Oct;26(7):809-815. doi: 10.1007/s00775-021-01897-1. Epub , 2021 Aug 30. PMID:34459989<ref>PMID:34459989</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ofg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alshanski I]] | [[Category: Alshanski I]] | ||
Revision as of 11:17, 14 June 2023
Oxytocin NMR solution structure
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