6DK5
The X-ray crystal structure of human endothelin-1, a polypeptide hormone regulator of blood pressure
Summary for 6DK5
| Entry DOI | 10.2210/pdb6dk5/pdb |
| Descriptor | Endothelin-1 (2 entities in total) |
| Functional Keywords | blood pressure, vasoconstrictor, sarafotoxins, polypeptide, hypertension, diabetes, stroke, hormone |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 4995.90 |
| Authors | McPherson, A. (deposition date: 2018-05-28, release date: 2019-01-02, Last modification date: 2024-11-20) |
| Primary citation | McPherson, A.,Larson, S.B. The X-ray crystal structure of human endothelin 1, a polypeptide hormone regulator of blood pressure. Acta Crystallogr F Struct Biol Commun, 75:47-53, 2019 Cited by PubMed Abstract: 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 P622, 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 P6 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 Å resolution, a model containing 25 waters was refined to 1.85 Å resolution with an R of 0.216 and an R 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. PubMed: 30605125DOI: 10.1107/S2053230X18016011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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