Literature summary for 3.6.4.B10 extracted from

Araki, K.; Suenaga, A.; Kusano, H.; Tanaka, R.; Hatta, T.; Natsume, T.; Fukui, K.
Functional profiling of asymmetrically-organized human CCT/TRiC chaperonin (2016), Biochem. Biophys. Res. Commun., 481, 232-238 .

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Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990	genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta	-

Subunits

Subunits	Comment	Organism
octamer	molecular organization of the eukaryote chaperonin known as CCT/TRiC complex, overview. Analysis of closed and open states of CCT complex, using molecular dynamics. The inter-subunit interaction energies are asymmetrically distributed and are remodeled during conformational changes of CCT complex. Exploration of redox related characteristics indicate changes in inner surface properties, including electrostatic potential, pKa and exposure of inner cysteine thiol groups, between the closed and open states	Homo sapiens

Synonyms

Synonyms	Comment	Organism
CCT/TRiC complex	-	Homo sapiens

General Information

General Information	Comment	Organism
additional information	eight distinct subunits are uniquely organized, providing a favorable folding cavity for specific client proteins such as tubulin and actin. Because of its heterogeneous subunit composition, CCT complex has polarized inner faces, which may underlie an essential part of its chaperonin function. Molecular organization of the eukaryote chaperonin known as CCT/TRiC complex, overview. Dynamics-based structural profiling of asymmetrically oriented chaperonin function	Homo sapiens

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Release 2023.1 (January 2023)