ATP binds G-protein beta associated TRiC/CCT

Stable Identifier
R-HSA-6814124
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
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ATP binds G-protein beta associated TRiC/CCT
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Based on structural studies of the TRiC/CCT chaperonin complex, the exchange of ADP for ATP enables conformational change of the chaperonin complex needed for folding of substrate proteins. It is assumed that TRiC/CCT-mediated folding of the G-protein beta subunit follows this universal pattern of TRiC/CCT functioning (Melki et al. 1997).

Literature References
PubMed ID Title Journal Year
9153422 Cytoplasmic chaperonin containing TCP-1: structural and functional characterization

Melki, R, Batelier, G, Soulié, S, Williams RC, Jr

Biochemistry 1997
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Authored
Orlic-Milacic, M  (2015-11-30)
Reviewed
Willardson, BM  (2015-12-22)
Created
Orlic-Milacic, M  (2015-11-25)
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