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Showing 1 to 3 of 3 for “"chaperonin containing TCP-1"”.
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The Mechanism of Assembly of the G-Protein Beta Gamma Subunit Dimer by CK2 Phosphorylated Phosducin-Like Protein and the Chaperonin Containing TCP-1
… PhLP has also been shown to interact with the chaperonin containing TCP-1 (CCT) atop its apical domain, not entering the substrate folding cavity. However, the physiological role of the PhLP-CCT interaction in G-protein beta gamma dimer formation remains unclear. This study addresses the …
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The Role of Phosducin-like Protein as a Co-chaperone with the Cytosolic Chaperonin Complex in Assembly of the G Protein βγ Subunit Dimer
… has been shown to interact with the cytosolic chaperonin containing TCP-1 (CCT), and the βγ subunit dimer of heterotrimeric G proteins (Gβγ). Here we provide details obtained from cryo-electron microscopic and biochemical studies on the structure of the complex between the cytosolic chaperonin …
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Assembly and substrate recognition properties of human CCT subunits of the TRiC chaperonin
Group II chaperonins are large multi-subunit complexes that fold cytosolic proteins to their native structures. They are composed of two back-to-back rings of 7-9 subunits. The eukaryotic cytosolic type II chaperonin Tailless Complex Polypeptide-1 (TCP-1) Ring Complex (TRiC) consists of eight …