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PMID: 266179 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Relative conformational rigidity in oxytocin and (1-penicillamine)-oxytocin: a proposal for the relationship of conformational flexibility to peptide hormone agonism and antagonism.

Meraldi JP, Hruby VJ, Brewster AI

Abstract

A comparative study of the proton and carbon-13 nuclear magnetic resonance spectral parameters of the peptide hormone oxytocin and of its competitive inhibitor [1-L-penicillamine]oxytocin has been made, and the results analyzed in terms of comparative conformational and dynamic properties. The results indicate that oxytocin has a flexible conformation, while [1-L-penicillamine]oxytocin has a more restricted conformation. The results provide a framework for understanding the mechanism of peptide hormone agonism and antagonism for these compounds, and an approach for understanding some features of the interaction of the hormone and related compounds with their receptor.

MeSH Terms
Binding Sites Magnetic Resonance Spectroscopy Oxytocin/analogs & derivatives,antagonists & inhibitors Penicillamine Protein Binding Protein Conformation
Chemicals
Oxytocin Penicillamine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Meraldi J P
Hruby V J
Brewster A I
References (26)
26 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1977-04-00
Pages
1373-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430763
Subset
IM
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