TRiC/CCT binds unfolded G-protein beta subunit

Stable Identifier
Reaction [binding]
Homo sapiens
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The TRiC/CCT chaperonin complex binds nascent, unfolded, G-protein beta subunit (GNB1, GNB2, GNB3, GNB4 or GNB5) (Wells et al. 2006). G-beta reaches a near-native state in the folding cavity of TRiC, except that TRiC cannot mediate the folding of the seven-bladed beta propeller of the G-protein beta to a stable conformation (Plimpton et al. 2015).

Literature References
PubMed ID Title Journal Year
25675501 Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly

Plimpton, RL, Cuellar, J, Lai, CW, Aoba, T, Makaju, A, Franklin, S, Mathis, AD, Prince, JT, Carrascosa, JL, Valpuesta, JM, Willardson, BM

Proc. Natl. Acad. Sci. U.S.A. 2015
16702223 Role of the chaperonin CCT/TRiC complex in G protein betagamma-dimer assembly

Wells, CA, Dingus, J, Hildebrandt, JD

J. Biol. Chem. 2006
Participant Of
Orthologous Events
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