SOLUTION CONFORMATION OF ENDOTHELIN, A POTENT VASO-CONSTRICTING BICYCLIC PEPTIDE - A COMBINED USE OF H-1-NMR SPECTROSCOPY AND DISTANCE GEOMETRY CALCULATIONS

被引：42

作者：

MUNRO, S

CRAIK, D

MCCONVILLE, C

HALL, J

SEARLE, M

BICKNELL, W

SCANLON, D

CHANDLER, C

机构：

[1] SWINBURNE LTD,NSITC,HAWTHORN,AUSTRALIA

[2] PETER MACCALLUM CANC INST,NMR FACIL,MELBOURNE,AUSTRALIA

[3] AUSPEP PTY LTD,PARKVILLE,AUSTRALIA

来源：

FEBS LETTERS | 1991年 / 278卷 / 01期

关键词：

ENDOTHELIN; VASOACTIVE PEPTIDE; DISTANCE GEOMETRY; H-1; NMR; 3-DIMENSIONAL CONFORMATION;

D O I：

10.1016/0014-5793(91)80071-A

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The solution structure of endothelin-1, a newly discovered potent bicyclic peptide vaso-constrictor agent, has been investigated using H-1 NMR conformational constraints and distance geometry calculations. The conformation is constrained by two disulphide bridges between Cys1-Cys15 and Cys3-Cys11 but the NMR data and computed conformers show additional helical structure between residues Leu6 and Cys11. Our results are compared with previous conflicting reports on the solution conformation of this peptide.

引用

页码：9 / 13

页数：5