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The conformational change in rhomboid protease GlpG induced by inhibitor binding to its S’-subsites
Rhomboid protease conducts proteolysis inside the hydrophobic environment of the membrane. The conformational flexibility of the protease is essential for the enzyme mechanism, but the nature of this flexibility is not completely understood. Here we describe the crystal structure of rhomboid proteas...
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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
2012
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3351039/ https://ncbi.nlm.nih.gov/pubmed/22515733 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi300368b |
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