The WD-repeat family of proteins is a large family of proteins whose members are structurally homologous but functionally diverse.
The WD-repeat motif is defined by four or more repeating units of a conserved core of 40-60 amino acids that begins with a glycine-histidine (GH) dipeptide and ends with a tryptophan-aspartic acid (WD) dipeptide. Regions within the WD-repeat exhibit sequence heterogeneity and are likely responsible for imparting their functional diversity. WD-repeat-containing proteins perform in a spectrum of cellular activities which includes RNA processing, signal transduction, transcription, vesicular trafficking, cytoskeletal assembly, chromatin assembly, and various aspects of cell division. It is also a seven times repeated part of beta subunits of GPCRs.
The crystal structure of the beta subunit of the heterotrimeric G-protein has been resolved and has provided a structural characterization of the WD-repeat. Each of the seven repeats of the G-protein beta subunit folds into small antiparallel beta-sheets that radiate from a central pseudo-symmetrical axis to form a beta propeller structure. The surfaces formed by the beta propeller structure are proposed to function as a scaffold capable of coordinating reversible protein-protein interactions.
Protein-protein interactions provide a source of complexity for the multitude of physiological processes that must be executed by eukaryotes for development and for the maintenance of homeostasis. Through their conserved beta propeller structure, WD-repeat-containing proteins contribute to this source of complexity and have thus established themselves as a critical subject of study.
Bethyl Laboratories Portfolio of Antibodies to members of the WD-repeat Family
CAF-1 p60 Antibodies
Coronin 1 Antibodies
Coronin 2 Antibodies
You find many of these this and more info in this WD Repeat Family of Proteins two page pdf document (122 kB).
Meanwhile there have been some additions to this product line meanwhile, click here for the newest list of WDR antibodies and control peptides.
In the Science issue of January 30th, 2009 Venteicher et al. identified WDR79 to be instrumental to the localization of telomerase to Cajal bodies as well as its delivery to the telomeres during S-phase. There had been three known essential components of the active telomerase holoenzyme: dyskerin, TERT (telomerase RT), and TERC (telomerase RNA component). Venteicher and his colleagues definitively report that in search of proteins that interact with dyskerin, they have discovered a fourth component critical to the activity of the telomerase holoenzyme: WDR79 or TCAB1 (Telomerase-Cajal-Body-Protein-1) as they named it.
Bethyl Antibody Listing