A THEORETICAL-STUDY OF THE STRUCTURE OF BIG ENDOTHELIN

被引：10

作者：

MENZIANI, MC

COCCHI, M

DEBENEDETTI, PG

GILBERT, RG

RICHARDS, WG

ZAMAI, M

CAIOLFA, VR

机构：

[1] UNIV OXFORD,PHYS CHEM LAB,OXFORD,ENGLAND

[2] FARMITALIA CARLO ERBA SPA,DEPT CARDIOVASC,RES LABS,MILAN,ITALY

来源：

JOURNAL DE CHIMIE PHYSIQUE ET DE PHYSICO-CHIMIE BIOLOGIQUE | 1991年 / 88卷 / 11-12期

关键词：

BIG ENDOTHELIN; MODELING; MOLECULAR DYNAMICS; 3D STRUCTURE;

D O I：

10.1051/jcp/1991882687

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：

Protein structure prediction and molecular dynamics simulations have been applied for elaborating the three dimensional structure of Big Endothelin (bigET). BigET is 38-amino acid peptide which is converted, by proteolytic cleavage, into Endothelin, the most potent and long lasting endothelium derived contracting factor identified up to date. The intervention of a specific, yet unknown, protease has been evoked. The determination of bigET tertiary structure will contribute to elucidate its proteolytic conversion. In-vitro experimental data on proteolytic fragmentation of bigET in the presence of known proteases and protein homogenates from endothelial cells have been considered for testing the proposed structure.

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页码：2687 / 2694

页数：8

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