The solution structure of sarafotoxin-c: implications for ligand recognition by endothelin

Mills, Robyn G., Ralston, Greg B. and King, Glenn F. (1994) The solution structure of sarafotoxin-c: implications for ligand recognition by endothelin. Journal of Biological Chemistry, 269 38: 23413-23419.

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Author Mills, Robyn G.
Ralston, Greg B.
King, Glenn F.
Title The solution structure of sarafotoxin-c: implications for ligand recognition by endothelin
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 1994-09-23
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 269
Issue 38
Start page 23413
End page 23419
Total pages 7
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
The solution structure of sarafotoxin-c has been determined using NMR spectroscopy. A total of 112 interproton distance constraints derived from two-dimensional NMR spectra were used to calculate a family of structures using a combination of distance geometry and dynamical simulated annealing calculations. The structures reveal a well defined α-helix extending from Glu9 to Cys15 and an N-terminal region (Cys1-Asp8) that is tightly constrained by disulfide bonds to Cys residues in the central helix. In contrast, the C-terminal region (His16-Trp21) does not adopt a defined conformation in the final family of structures. This is consistent with the paucity of NMR-derived structural constraints obtained for this region and leads to the suggestion that the C-terminal region oscillates rapidly between a number of substantially different conformers. It is proposed that differences between the central helix of the endothelin and sarafotoxin isopeptides might be important in binding of these ligands by the G protein-coupled endothelin receptors.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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