Crystal structure of XMRV protease differs from the structures of other retropepsins
| Title | Crystal structure of XMRV protease differs from the structures of other retropepsins |
| Publication Type | Journal Article |
| Year of Publication | 2011 |
| Authors | Li, M., DiMaio F., Zhou D., Gustchina A., Lubkowski J., Dauter Z., Baker D., & Wlodawer A. |
| Journal | Nature structural & molecular biology |
| Volume | 18 |
| Issue | 2 |
| Pagination | 227-9 |
| Date Published | 2011 Feb |
| ISSN | 1545-9985 |
| Keywords | Amino 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 Journal | Nat. Struct. Mol. Biol. |
| Attachment | Size |
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| li11A.pdf | 663.49 KB |