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Solution conformation of CCK9, a cholecystokinin analog.

作者信息

Moroder L, D'Ursi A, Picone D, Amodeo P, Temussi P A

机构信息

MPI für Biochemie, Martinsried bei München, Germany.

出版信息

Biochem Biophys Res Commun. 1993 Feb 15;190(3):741-6. doi: 10.1006/bbrc.1993.1111.

DOI:10.1006/bbrc.1993.1111
PMID:8094956
Abstract

Cholecystokinin (CCK) is a peptide hormone endowed with several important biological activities, both in the central and peripheral nervous system. Previous conformational studies have dealt mainly with its C-terminal octapeptide fragment (CCK8), which represents the shortest fully circulating form of this hormone. We have undertaken a detailed NMR conformational study in a DMSOd6/H2O cryomixture at 278 K of the CCK analog H-Arg-Asp-Tyr(SO3H)-Thr-Gly-Trp-Nle-Asp-PheNH2 (CCK9) which retains all the bioactivities of CCK8, but was found to be remarkably more stable in acidic media and unaffected by air oxidation due to Met replacements. The predominant conformation contains a gamma-turn centered on Thr4, separated by Gly5 from a helical segment that comprises the C-terminal residues.

摘要

相似文献

1
Solution conformation of CCK9, a cholecystokinin analog.
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2
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The micelle-associated 3D structures of Boc-Y(SO3)-Nle-G-W-Nle-D-2-phenylethylester (JMV-180) and CCK-8(s) share conformational elements of a calculated CCK1 receptor-bound model.Boc-Y(SO3)-Nle-G-W-Nle-D-2-苯乙酯（JMV-180）与胶束相关的三维结构和CCK-8(s)共享计算得出的CCK1受体结合模型的构象元件。
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