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

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

Author information

1
Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland, USA.

Abstract

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.

PMID:
21258323
PMCID:
PMC3058223
DOI:
10.1038/nsmb.1964
[Indexed for MEDLINE]
Free PMC Article

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