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

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.

SUBMITTER: Li M 

PROVIDER: S-EPMC3058223 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature