LearnCoil-VMF: computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins

J Mol Biol. 1999 Jul 30;290(5):1031-41. doi: 10.1006/jmbi.1999.2796.

Abstract

Crystallographic studies have shown that the coiled-coil motif occurs in several viral membrane-fusion proteins, including HIV-1 gp41 and influenza virus hemagglutinin. Here, the LearnCoil-VMF program was designed as a specialized program for identifying coiled-coil-like regions in viral membrane-fusion proteins. Based upon the use of LearnCoil-VMF, as well as other computational tools, we report detailed sequence analyses of coiled-coil-like regions in retrovirus, paramyxovirus and filovirus membrane-fusion proteins. Additionally, sequence analyses of these proteins outside their putative coiled-coil domains illustrate some structural differences between them. Complementing previous crystallographic studies, the coiled-coil-like regions detected by LearnCoil-VMF provide further evidence that the three-stranded coiled coil is a common motif found in many diverse viral membrane-fusion proteins. The abundance and structural conservation of this motif, even in the absence of sequence homology, suggests that it is critical for viral-cellular membrane fusion. The LearnCoil-VMF program is available at http://web.wi.mit.edu/kim

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Computer Simulation*
  • Conserved Sequence
  • Databases, Factual
  • Filoviridae / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Respirovirus / chemistry
  • Retroviridae / chemistry
  • Sequence Analysis
  • Software*
  • Viral Fusion Proteins / chemistry*
  • Viral Fusion Proteins / genetics

Substances

  • Viral Fusion Proteins