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| | ==The X-ray crystal structure of human endothelin-1, a polypeptide hormone regulator of blood pressure== | | ==The X-ray crystal structure of human endothelin-1, a polypeptide hormone regulator of blood pressure== |
| - | <StructureSection load='6dk5' size='340' side='right' caption='[[6dk5]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='6dk5' size='340' side='right'caption='[[6dk5]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6dk5]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DK5 FirstGlance]. <br> | + | <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> |
| - | </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=6dk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dk5 OCA], [http://pdbe.org/6dk5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dk5 RCSB], [http://www.ebi.ac.uk/pdbsum/6dk5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dk5 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</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=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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EDN1_HUMAN EDN1_HUMAN]] Endothelins are endothelium-derived vasoconstrictor peptides. | + | [https://www.uniprot.org/uniprot/EDN1_HUMAN EDN1_HUMAN] Endothelins are endothelium-derived vasoconstrictor peptides. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: McPherson, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Blood pressure]] | + | [[Category: McPherson A]] |
| - | [[Category: Diabetes]]
| + | |
| - | [[Category: Hormone]]
| + | |
| - | [[Category: Hypertension]]
| + | |
| - | [[Category: Polypeptide]]
| + | |
| - | [[Category: Sarafotoxin]]
| + | |
| - | [[Category: Stroke]]
| + | |
| - | [[Category: Vasoconstrictor]]
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| Structural highlights
Function
EDN1_HUMAN Endothelins are endothelium-derived vasoconstrictor peptides.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McPherson A, Larson SB. The X-ray crystal structure of human endothelin 1, a polypeptide hormone regulator of blood pressure. Acta Crystallogr F Struct Biol Commun. 2019 Jan 1;75(Pt 1):47-53. doi:, 10.1107/S2053230X18016011. Epub 2019 Jan 1. PMID:30605125 doi:http://dx.doi.org/10.1107/S2053230X18016011
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