Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin.

Journal article

Protein folding is assisted by molecular chaperones. CCT (chaperonin containing TCP-1, or TRiC) is a 1-MDa oligomer that is built by two rings comprising eight different 60-kDa subunits. This chaperonin regulates the folding of important proteins including actin, α-tubulin and β-tubulin. We used an electron density map at 5.5 Å resolution to reconstruct CCT, which showed a substrate in the inner cavities of both rings. Here we present the crystal structure of the open conformation of this nan...

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Authors: Muñoz, I; Yébenes, H; Zhou, M; Mesa, P; Serna, M

• Publication status: Published
• Journal: Nature structural and molecular biology
• Volume: 18
• Issue: 1
• Pages: 14-19
• Publication date: 2011-01-01
• DOI: 10.1038/nsmb.1971
• EISSN: 1545-9985
• ISSN: 1545-9993
• Language: English
• Keywords: Crystallography, X-Ray; Models, Molecular; Cattle; Binding Sites; Animals; Protein Subunits; Mass Spectrometry; Tubulin; Protein Structure, Tertiary; Protein Folding; Chaperonin Containing TCP-1