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

TitleCrystal structure of XMRV protease differs from the structures of other retropepsins
Publication TypeJournal Article
Year of Publication2011
AuthorsLi, M., DiMaio F., Zhou D., Gustchina A., Lubkowski J., Dauter Z., Baker D., & Wlodawer A.
JournalNature structural & molecular biology
Volume18
Issue2
Pagination227-9
Date Published2011 Feb
ISSN1545-9985
KeywordsAmino Acid Sequence, Collaborative Publication, Crystallography, X-Ray, Molecular Sequence Data, Peptide Hydrolases, Protein Multimerization, Viral Proteins, Xenotropic murine leukemia virus-related virus
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.

Alternate JournalNat. Struct. Mol. Biol.
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