Crystal structure of XMRV protease differs from the structures of other retropepsins.
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ABSTRACT:
SUBMITTER: Li M
PROVIDER: S-EPMC3058223 | biostudies-literature | 2011 Feb
REPOSITORIES: biostudies-literature
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Crystal structure of XMRV protease differs from the structures of other retropepsins.
Li Mi M Dimaio Frank F Zhou Dongwen D Gustchina Alla A Lubkowski Jacek J Dauter Zbigniew Z Baker David D Wlodawer Alexander A
Nature structural & molecular biology 20110123 2
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. ...[more]
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