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6dk5

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'''Unreleased structure'''
 
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The entry 6dk5 is ON HOLD
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==The X-ray crystal structure of human endothelin-1, a polypeptide hormone regulator of blood pressure==
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<StructureSection load='6dk5' size='340' side='right'caption='[[6dk5]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6dk5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DK5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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=6dk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dk5 OCA], [https://pdbe.org/6dk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dk5 RCSB], [https://www.ebi.ac.uk/pdbsum/6dk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dk5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EDN1_HUMAN EDN1_HUMAN] Endothelins are endothelium-derived vasoconstrictor peptides.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human endothelin is a 21-amino-acid polypeptide, constrained by two intra-chain disulfide bridges, that is made by endothelial cells. It is the most potent vasoconstrictor in the body and is crucially important in the regulation of blood pressure. It plays a major role in a host of medical conditions, including hypertension, diabetes, stroke and cancer. Endothelin was crystallized 28 years ago in the putative space group P6122, but the structure was never successfully solved by X-ray diffraction. Using X-ray diffraction data from 1992, the structure has now been solved. Assuming a unit cell belonging to space group P61 and a twin fraction of 0.28, a solution emerged with two, almost identical, closely associated molecules in the asymmetric unit. Although the data extended to beyond 1.8 A resolution, a model containing 25 waters was refined to 1.85 A resolution with an R of 0.216 and an Rfree of 0.284. The disulfide-constrained `core' of the molecule, amino-acid residues 1-15, has a main-chain conformation that is essentially the same as endothelin when bound to its receptor, but many side-chain rotamers are different. The carboxy-terminal `tail' comprising amino-acid residues 16-21 is extended as when receptor-bound, but it exhibits a different conformation with respect to the `core'. The dimer that comprises the asymmetric unit is maintained almost exclusively by hydrophobic interactions and may be stable in an aqueous medium.
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Authors: McPherson, A., McPherson, A.
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The X-ray crystal structure of human endothelin 1, a polypeptide hormone regulator of blood pressure.,McPherson A, Larson SB Acta Crystallogr F Struct Biol Commun. 2019 Jan 1;75(Pt 1):47-53. doi:, 10.1107/S2053230X18016011. Epub 2019 Jan 1. PMID:30605125<ref>PMID:30605125</ref>
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Description: The X-ray crystal structure of human endothelia-1, a polypeptide hormone regulator of blood pressure
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Mcpherson, A]]
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<div class="pdbe-citations 6dk5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: McPherson A]]

Current revision

The X-ray crystal structure of human endothelin-1, a polypeptide hormone regulator of blood pressure

PDB ID 6dk5

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