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

Using energy and density guided Rosetta refinement to improve molecular replacement, we have determined the crystal structure of the protease (PR) encoded by xenotropic murine leukemia virus-related virus (XMRV). Despite overall similarity of XMRV PR to other retropepsins, the topology of its dimer...

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Autores principales: Li, Mi, DiMaio, Frank, Zhou, Dongwen, Gustchina, Alla, Lubkowski, Jacek, Dauter, Zbigniew, Baker, David, Wlodawer, Alexander
Formato: Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3058223/
https://www.ncbi.nlm.nih.gov/pubmed/21258323
http://dx.doi.org/10.1038/nsmb.1964
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author Li, Mi
DiMaio, Frank
Zhou, Dongwen
Gustchina, Alla
Lubkowski, Jacek
Dauter, Zbigniew
Baker, David
Wlodawer, Alexander
author_facet Li, Mi
DiMaio, Frank
Zhou, Dongwen
Gustchina, Alla
Lubkowski, Jacek
Dauter, Zbigniew
Baker, David
Wlodawer, Alexander
author_sort Li, Mi
collection PubMed
description Using energy and density guided Rosetta refinement to improve molecular replacement, we have determined the crystal structure of the protease (PR) encoded by xenotropic murine leukemia virus-related virus (XMRV). Despite overall similarity of XMRV PR to other retropepsins, the topology of its dimer interface more closely resembles the monomeric, pepsin-like enzymes. Thus, XMRV PR may represent a distinct evolutionary branch of the family of aspartic proteases.
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spelling pubmed-30582232011-08-01 Crystal structure of XMRV protease differs from the structures of other retropepsins Li, Mi DiMaio, Frank Zhou, Dongwen Gustchina, Alla Lubkowski, Jacek Dauter, Zbigniew Baker, David Wlodawer, Alexander Nat Struct Mol Biol Article Using energy and density guided Rosetta refinement to improve molecular replacement, we have determined the crystal structure of the protease (PR) encoded by xenotropic murine leukemia virus-related virus (XMRV). Despite overall similarity of XMRV PR to other retropepsins, the topology of its dimer interface more closely resembles the monomeric, pepsin-like enzymes. Thus, XMRV PR may represent a distinct evolutionary branch of the family of aspartic proteases. 2011-01-23 2011-02 /pmc/articles/PMC3058223/ /pubmed/21258323 http://dx.doi.org/10.1038/nsmb.1964 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Li, Mi
DiMaio, Frank
Zhou, Dongwen
Gustchina, Alla
Lubkowski, Jacek
Dauter, Zbigniew
Baker, David
Wlodawer, Alexander
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
title_full Crystal structure of XMRV protease differs from the structures of other retropepsins
title_fullStr Crystal structure of XMRV protease differs from the structures of other retropepsins
title_full_unstemmed Crystal structure of XMRV protease differs from the structures of other retropepsins
title_short Crystal structure of XMRV protease differs from the structures of other retropepsins
title_sort crystal structure of xmrv protease differs from the structures of other retropepsins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3058223/
https://www.ncbi.nlm.nih.gov/pubmed/21258323
http://dx.doi.org/10.1038/nsmb.1964
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