Implications of the X-ray structure of deamino-oxytocin to agonist/antagonist-receptor interactions

Victor J. Hruby

doi:10.1016/0165-6147(87)90142-8

Implications of the X-ray structure of deamino-oxytocin to agonist/antagonist-receptor interactions

Victor J. Hruby

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

50 Scopus citations

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	https://doi.org/10.1016/0165-6147(87)90142-8
State	Published - Sep 1987

ASJC Scopus subject areas

Toxicology
Pharmacology

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10.1016/0165-6147(87)90142-8

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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.",

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AB - 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.

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Implications of the X-ray structure of deamino-oxytocin to agonist/antagonist-receptor interactions

Abstract

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