title: A comparison of X-ray and NMR structures for human endothelin-1.
abstract: Direct comparisons between the recently solved X-ray and NMR structures of human endothelin-1 with respect to secondary structure, RMS deviations, surface accessibilities, and side-chain conformers indicate important differences in conformation, especially in the C-terminus, but also in the central loop region, that are important for defining the specificity of binding. These differences are larger than seen for other X-ray and NMR structures that have been compared. Comparisons between the X-ray structure and the NMR NOE constraints highlight the regions of flexibility and environment-induced diversity in the endothelin structures.
authors.affiliation: Department of Crystallography, Birkbeck College, University of London, United Kingdom.
authors.forename: B A
authors.initials: BA
authors.lastname: Wallace
authors.forename: R W
authors.initials: RW
authors.lastname: Janes
authors.forename: D A
authors.initials: DA
authors.lastname: Bassolino
authors.forename: S R
authors.initials: SR
authors.lastname: Krystek
mesh_terms: D003196:Computer Graphics; D018360:Crystallography, X-Ray; D016232:Endothelins / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D016232:Endothelins