The crystal structure of human endothelin.
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.
Janes
R W
RW
Department of Crystallography, Birkbeck College, University of London, UK.
Peapus
D H
DH
Wallace
B A
BA
D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D016232:Endothelins / Q000737:chemistry*; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits; D051381:Rats; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012997:Solvents / Q000494:pharmacology; D013552:Swine; D014757:Viper Venoms / Q000737:chemistry
D016232:Endothelins; D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D012997:Solvents; D014757:Viper Venoms; C078887:bibrotoxin; C057354:sarafotoxins s6