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Spiricoil uses protein domain annotation to predict coiled coil presence and oligormeric state for all completely sequenced organisms; CC+ Archived 2011-11-08 at the Wayback Machine is a relational database of coiled coils found in the PDB
CCDC25 was shown by a yeast-two-hybrid assay to interact with Smad2, a latent transcription factor that is part of the TGF-β signaling pathway. [9] The protein is a predicted substrate of Casein Kinase 1, Casein Kinase 2, cGMP-dependent protein kinase, and the Insulin Receptor; all of which have well defined roles in cell signaling.
Coiled-coil research began in 1953 when Dr. Francis Crick first reported on the theory behind the packing formation of α-helices in fibrous proteins at the time, which he proposed to consist of alpha helices composed of heptad repeats, or seven-residue repeats (a-b-c-d-e-f-g), whereby 2 or more alpha helices twist around each other similar to the strands of a rope. [2]
B-box domains are found in over 1500 proteins from a variety of organisms. They are found in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). TRIM proteins contain a type 2 B-box domain ...
CCDC188 protein is 402 amino acids long and is 4.3 kDa. [17] The protein contains a leucine zipper and transmembrane domain . [ 18 ] The presence of both a leucine zipper domain and transmembrane domain suggests that CCDC188 protein functions as a transcription factor that is tightly regulated and must be cleaved out of a membrane to be activated.
Coiled-Coil Domain Containing protein 82 (CCDC82) is a protein that in humans, is encoded for by the gene of the same name, CCDC82. The CCDC82 gene is expressed in nearly all of human tissues at somewhat low rates. As of today, there are no patents involving CCDC82 and the function remains unknown.
The CARD-CC protein family is defined by an evolutionary conserved "caspase activation and recruitment domain" and a coiled-coil (CC) domain. [1] [2] Coiled-coils (CC) act as oligomerization domains for many proteins such as structural and motor proteins, and transcription factors. This means that monomers are converted to macromolecular ...
The protein has 17 predicted alpha helices sites, a characteristic of coiled-coil proteins, and 1 predicted beta-pleated sheet. The following image shows the predicted regions of alpha helices and beta pleated sheets by two programs STRAP [ 9 ] and Quickphyre: [ 10 ] Note: the consensus secondary structures are shown.
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