Abstract
Abstract: A recent Science article demonstrating the X-ray structure of an oxytocin analog indicates low-energy interconversion of the disulfide between a right-handed and left-handed helicity, as well as conformational flexibility for the side-chain Asn5 and Ile3 residues. These results and other corresponding biological data support a hypothesis which, Victor Hruby explains, suggests that oxytocin antagonist analogs interact with the oxytocin receptor in a different manner to the interaction of oxytocin agonists. This may have general implications for agonist/antagonist interactions and may aid rational analog design.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 336-339 |
| Number of pages | 4 |
| Journal | Trends in Pharmacological Sciences |
| Volume | 8 |
| Issue number | 9 |
| DOIs | |
| State | Published - Sep 1987 |
ASJC Scopus subject areas
- Toxicology
- Pharmacology