Chaperonin Cpn60/GroEL/TCP-1 family
IPR002423
Definition
The assembly of proteins has been thought to be the sole result of properties inherent in the primary sequence of polypeptides themselves. In some cases, however, structural information from other protein molecules is required for correct folding and subsequent assembly into oligomers PMID:2897629. These 'helper' molecules are referred to as molecular chaperones, a subfamily of which are the chaperonins PMID:1349837, which include 10kDa and 60kDa proteins. These are found in abundance in prokaryotes, chloroplasts and mitochondria. They are required for normal cell growth (as demonstrated by the fact that no temperature sensitive mutants for the chaperonin genes can be found in the temperature range 20 to 43 degrees centigrade PMID:2897629), and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions PMID:1349837. The 10kDa chaperonin (Cpn10) and its bacterial homologue groES, exist as a ring-shaped oligomer of between 6 to 8 identical subunits, whereas the 60kDa chaperonin (Cpn60) and its bacterial homologue groEL, form a structure comprising 2 stacked rings, each ring containing 7 identical subunits PMID:2897629. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The Cpn10 and Cpn60 oligomers also require Mg2+-ATP in order to interact to form a functional complex, although the mechanism of this interaction is as yet unknown PMID:1350777. This chaperonin complex is essential for the correct folding and assembly of polypeptides into oligomeric structures, of which the chaperonins themselves are not a part PMID:1349837. The binding of Cpn10 to Cpn60 inhibits the weak ATPase activity of Cpn60. TCP-1 (t-complex polypeptide 1) is a subunit of the hetero-oligomeric complex CCT (chaperonin containing TCP- 1) present in the eukaryotic cytosol. It is a member of the chaperonin family which includes GroEL, 60kDa heat shock protein (Hsp60), Rubisco subunit binding protein (RBP) and thermophilic factor 55 (TF55) PMID:7601114. BBS10 and BBS10 chaperonins play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia PMID:20080638.
16 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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