7ofg

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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 ==
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<table><tr><td colspan='2'>Full crystallographic 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>
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<table><tr><td colspan='2'>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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 14 models</td></tr>
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<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>
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<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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7ofg" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

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Oxytocin NMR solution structure

PDB ID 7ofg

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