Crystal structure of XMRV protease differs from the structures of other retropepsins

Nat Struct Mol Biol. 2011 Feb;18(2):227-9. doi: 10.1038/nsmb.1964. Epub 2011 Jan 23.


Using energy and density guided Rosetta refinement to improve molecular replacement, we determined the crystal structure of the protease encoded by xenotropic murine leukemia virus-related virus (XMRV). Despite overall similarity of XMRV protease to other retropepsins, the topology of its dimer interface more closely resembles those of the monomeric, pepsin-like enzymes. Thus, XMRV protease may represent a distinct branch of the aspartic protease family.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Peptide Hydrolases / chemistry*
  • Protein Multimerization
  • Viral Proteins / chemistry*
  • Xenotropic murine leukemia virus-related virus / chemistry
  • Xenotropic murine leukemia virus-related virus / enzymology*


  • Viral Proteins
  • Peptide Hydrolases