Format

Send to

Choose Destination
FEBS Lett. 2004 Jul 2;569(1-3):261-6.

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

Author information

1
Unidad de Biofísica (CSIC-UPV/EHU) y Departamento de Bioquímica, Universidad del País Vasco, Aptdo. 644, 48080 Bilbao, Spain.

Abstract

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 EBOwt (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.

PMID:
15225645
DOI:
10.1016/j.febslet.2004.06.006
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center