D Domain
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D Domain
D-domain (Dimerization domain) is found in the upstream of the F-box domain, which is a conserved dimerization motif located in WD40 repeat F box proteins, such as Cdc4, Met30, β-TrCP and Pop1/2. But Vts1, a RNA binding protein at the SAM domain found in yeast contain D-domain though it does not have any F-box domain. As targeting domain or docking site, D-domain is found in the ETS-domain transcription factor Elk-1. It is distinct from the phospho-acceptor motifs and plays a crucial function in the efficient phosphorylation and activation of Elk-1 by MAP kinases (MAPKs) such as extracellular signal-regulated protein kinase (ERK), JNK, mitogen and stress-activated protein kinase-1, and ribosomal S6 kinase. Additionally this domain can be incorporated into chimeric antigen receptor (CAR) designs for T cell therapies that allows for the specific recognition and binding of target antigens, such as CD123, which is a potential therapeutic target for hematologic malignancies li ...
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F-box Protein
F-box proteins are proteins containing at least one F-box domain. The first identified F-box protein is one of three components of the SCF complex, which mediates ubiquitination of proteins targeted for degradation by the 26S proteasome. Core components F-box domain is a protein structural motif of about 50 amino acids that mediates protein–protein interactions. It has consensus sequence and varies in few positions. It was first identified in cyclin F. The F-box motif of Skp2, consisting of three alpha-helices, interacts directly with the SCF protein Skp1. F-box domains commonly exist in proteins in cancer with other protein–protein interaction motifs such as leucine-rich repeats (illustrated in the Figure) and WD repeats, which are thought to mediate interactions with SCF substrates. Function F-box proteins have also been associated with cellular functions such as signal transduction and regulation of the cell cycle. In plants, many F-box proteins are represented in gene ...
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