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A Two-step Mechanism for the Folding of Actin by the Yeast Cytosolic Chaperonin
Actin requires the chaperonin containing TCP1 (CCT), a hexadecameric ATPase essential for cell viability in eukaryotes, to fold to its native state. Following binding of unfolded actin to CCT, the cavity of the chaperone closes and actin is folded and released in an ATP-dependent folding cycle. In y...
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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Society for Biochemistry and Molecular Biology
2011
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3012972/ https://ncbi.nlm.nih.gov/pubmed/21056978 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.166256 |
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