Ankyrin-repeat domains/proteins

I/cBa substrate peptide (Figure 7.11). These isolated j5-catenin and I/cBa peptides should accurately reflect the context of these destruction motifs in their respective full-length proteins, since Lysl9 and the destruction motif of j5-catenin are both in a 133-residue N-terminal region that has been previously shown to have a disordered structure by proteolytic digestion analysis [104]. The destruction motif of I/cBa similarly resides outside the structured ankyrin-repeat domain. 

Alternative substrates may exist for the PHDs proposed examples include RNA polymerase II and IkB kinase-P (which is negatively regulated by PHDl) (115, 116). However, unequivocal evidence (e.g., demonstration of hydroxylation by mass spectrometry) has not yet been demonstrated for these proteins. In contrast, FIH has been shown to catalyze hydroxylation of ankyrin repeat domain (ARD) proteins from the NFkB (nuclear factor kB) and Notch family at highly conserved as-paraginyl residues (117, 118). The ARD is a common protein motif, with over 200 human members of the ARD protein family being predicted. Evidence that ARD hydroxylation occurs frequently in human cells supports the assertion (117, 118) that posttranslational hydroxylation of cytoplasmic proteins in... 

The ankyrin repeat motif is one of the most common protein-protein interaction domains. Ankyrin repeats are modules of about 33 amino acids repeated in tandem. They are found in a large number of proteins with diverse cellular functions such as transcriptional regulators, signal transducers, cell-cycle regulators, and cytoskeletal proteins. 

The specific domains that recognize KMe have been described within several protein families the so-called "royal family" of Tudor, Agenet, chromo, PWWP, and MBT domains the plant homeodomain (PHD) the WD40 repeat protein—WDR5 and ankyrin repeats [37,38]. Given the rapid rate of progress in this area, the relatively low affinity of these interactions (Kd values typically 10-100 jjM), the wide variety of... 

Code for a domain that interacts with the muscle ankyrin repeat proteins... 

Fig. 1 The structure of a-LTX. (a) Schematic of a-LTX processing in the venom gland, (b) Primary and domain structure. The numbered boxes, ankyrin repeats (ARs). Grey, imperfect repeats C, conserved cysteines residues in the N-terminal domain open arrowhead, insert in the mutant a-LTXN4C. Protein domains identified from the 3D structure (Orlova et al. 2000) are delimited below, (c) 3D reconstructions of the a-LTX monomer, dimer and tetramer, viewed from the top and side. The monomer has been computationally extracted from the experimentally determined tetramer structure. Left-most image, a scheme of the monomer, with the domains designated by different shades of grey. Filled arrowhead, strong association of the head domains in the dimer.

ASPP Ankyrin-repeat, SH3-domain, and proline-rich region containing proteins... 

Ankyrin-Repeat A domain or motif, named after ankydrin, a cytoskeletal protein, is found in... 

Figure 32.35. Ankyrin Repeat Structure. Four ankyrin repeats are shown with one shown in red. These domains interact with other proteins, primarily through their loops. 

Figure 32.35 Ankyrin repeat structure. One ankyrin domain is shown in red in this series of four ankyrin repeats. Notice the hairpin loop followed by a helix-turn-helix motif in the red-colored ankyrin unit. Ankyrin domains interact with other proteins, primarily through their loops. [Drawn from lAWC,pdb.]...

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