Murine leukemia virus reverse transcriptase: structural comparison with HIV-1 reverse transcriptase

Virus Res. 2008 Jun;134(1-2):186-202. doi: 10.1016/j.virusres.2008.01.001. Epub 2008 Feb 21.

Abstract

Recent X-ray crystal structure determinations of Moloney murine leukemia virus reverse transcriptase (MoMLV RT) have allowed for more accurate structure/function comparisons to HIV-1 RT than were formerly possible. Previous biochemical studies of MoMLV RT in conjunction with knowledge of sequence homologies to HIV-1 RT and overall fold similarities to RTs in general, provided a foundation upon which to build. In addition, numerous crystal structures of the MoMLV RT fingers/palm subdomain had also shed light on one of the critical functions of the enzyme, specifically polymerization. Now in the advent of new structural information, more intricate examination of MoMLV RT in its entirety can be realized, and thus the comparisons with HIV-1 RT may be more critically elucidated. Here, we will review the similarities and differences between MoMLV RT and HIV-1 RT via structural analysis, and propose working models for the MoMLV RT based upon that information.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acid Sequence
  • HIV-1 / enzymology*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Moloney murine leukemia virus / enzymology*
  • Protein Structure, Tertiary
  • RNA-Directed DNA Polymerase / chemistry*
  • RNA-Directed DNA Polymerase / genetics
  • RNA-Directed DNA Polymerase / metabolism
  • Reverse Transcription
  • Ribonuclease H / chemistry
  • Ribonuclease H / metabolism
  • Sequence Alignment
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism

Substances

  • Viral Proteins
  • RNA-Directed DNA Polymerase
  • Ribonuclease H