T-complex protein 1
IPR017998
Definition
Protein folding is generally thought to result solely from properties inherent in the polypeptide primary sequence. However, additional proteins known as molecular chaperones are sometimes required to mediate correct folding and subsequent oligomer assembly PMID:2897629. These chaperones bind to specific protein surfaces, preventing incorrect folding and the formation of non-functional structures PMID:1487154.T-complex protein 1 (TCP-1) is a highly conserved cytosolic molecular chaperone PMID:1348353. TCP-1 has also been shown to associate with Golgi membranes and microtubules, the latter suggesting a role in mitotic spindle formation during cell division, particularly in sperm where it is highly abundant PMID:1836250. Structurally, TCP-1 forms a double-ring complex comprising 6-8 subunits per ring, similar to the architecture of the 10 kDa and 60 kDa chaperonins. The amino acid sequence shows significant similarity to the 60 kDa chaperonin and to TF55, a chaperone from the archaeon Sulfolobus shibatae PMID:1836250.
11 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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