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

Identifieur interne : 001A01 ( Istex/Curation ); précédent : 001A00; suivant : 001A02

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

Auteurs : Mi Li [États-Unis] ; Frank Dimaio [États-Unis] ; Dongwen Zhou [États-Unis] ; Alla Gustchina [États-Unis] ; Jacek Lubkowski [États-Unis] ; Zbigniew Dauter [États-Unis] ; David Baker [États-Unis] ; Alexander Wlodawer [États-Unis]

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RBID : ISTEX:81B60EC51965B864C1593E7AC49227EA89085376

Abstract

XMRV is a retrovirus that has been linked to prostate cancer and chronic fatigue syndrome. The crystal structure of the XMRV protease differs from the structures of other retropepsins and instead resembles those of pepsin-like enzymes, suggesting that this protease may represent a distinct evolutionary branch of the aspartic proteases.

Url:
DOI: 10.1038/nsmb.1964

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ISTEX:81B60EC51965B864C1593E7AC49227EA89085376

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<div type="abstract" xml:lang="eng">XMRV is a retrovirus that has been linked to prostate cancer and chronic fatigue syndrome. The crystal structure of the XMRV protease differs from the structures of other retropepsins and instead resembles those of pepsin-like enzymes, suggesting that this protease may represent a distinct evolutionary branch of the aspartic proteases.</div>
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