Roles of a conserved proline in the internal fusion peptide of Ebola glycoprotein

被引：28

作者：

Gómara, MJ

Mora, P

Mingarro, I

Nieva, JL

机构：

[1] Univ Basque Country, CSIC, EHU, Unidad Biofis, E-48080 Bilbao, Spain

[2] Univ Basque Country, Dept Bioquim, E-48080 Bilbao, Spain

[3] Univ Valencia, Dept Bioquim & Biol Mol, E-46100 Burjassot, Spain

来源：

FEBS LETTERS | 2004年 / 569卷 / 1-3期

关键词：

Ebola glycoprotein; viral fusion peptide; peptide-lipid interaction; peptide conformation; protein insertion into membranes; proline;

D O I：

10.1016/j.febslet.2004.06.006

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 structural determinants underlying the functionality of viral internal fusion peptides (IFPs) are not well understood. We have compared EBOwt (GAAIGLAWIPYFGPAAE), representing the IFP of the Ebola fusion protein GP, and EBOmut (GAAIGLAWIPYFGRAAE) derived from a non-functional mutant with conserved Pro537 substituted by Arg. P537R substitution did not abrogate peptide-membrane association, but interfered with the ability to induce bilayer destabilization. Structural determinations suggest that Pro537 is required to preserve a membrane-perturbing local conformation in apolar environments. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：261 / 266

页数：6

共 31 条

[21] Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin [J].