1EDN
HUMAN ENDOTHELIN-1
Summary for 1EDN
Entry DOI | 10.2210/pdb1edn/pdb |
Descriptor | ENDOTHELIN-1 (1 entity in total) |
Functional Keywords | signal polypeptide g-protein coupled-receptor ligand, vasoconstrictor |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 2497.95 |
Authors | Wallace, B.A.,Janes, R.W. (deposition date: 1994-09-19, release date: 1995-10-15, Last modification date: 2024-10-23) |
Primary citation | Janes, R.W.,Peapus, D.H.,Wallace, B.A. The crystal structure of human endothelin. Nat.Struct.Biol., 1:311-319, 1994 Cited by PubMed Abstract: The three-dimensional structure of the vasoactive polypeptide endothelin, the most potent vasoconstrictor yet identified, has been determined by X-ray crystallography to 2.18 A resolution. This intermediate-sized structure was solved by molecular replacement techniques using a fragment of an NMR-derived model for initial phasing of the data. However, comparisons of the final X-ray structure with the many diverse models derived from NMR data indicate some important differences, especially in the carboxy-terminal region of the molecule: the entire carboxy terminal tail (residues 16-21) is helical in the crystal structure, but not in any of the NMR structures. This may be a functionally significant difference as this region is crucial for receptor binding and vasoactivity. PubMed: 7664037DOI: 10.1038/nsb0594-311 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.18 Å) |
Structure validation
Download full validation report