Interaction domains

In order to bind to target proteins, adaptor proteins contain protein-protein interaction domains which recognize specific target motifs (Fig. 1). Through combinations of these domains, adaptor protein can interact with multiple... 

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. 

Protein-protein interaction domain that binds to short peptide motif at the C-terminal of target proteins. Particularly important in spatial organization of receptors and ion channels. 

Protein-protein interaction domain that recognizes short sequences containing a phosphotyrosine. Hydrophobic residues N-terminal to the phosphotyrosine residue provide distinction from SH2 domains. Particularly important in assembling protein complexes at activated receptors. 

Protein-protein interaction domain which, like SH3 domains, bind to polyproline sequences. 

Wyss S, Dimitrov AS, Baribaud F, Edwards TG, Blumenthal R, Hoxie JA. Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain in the gp41 cytoplasmic tail. J Virol 2005 79(19) 12231-12241. 

Pawson, T., and Nash, P. (2003) Assembly of cell regulatory systems through protein interaction domains. 

This spectrin network further binds to actin microfilaments and to numerous other ligands. These associations are probably dynamic. For example, phosphorylation of ankyrin can alter its affinity for spectrin. The functions of the multiple protein-interaction domains of both spectrin and ankyrin have been as yet only partially defined (see Ch. 8). 

It is noteworthy that Src-induced increase in NR1-NR2A receptor activity is promoted by the coexpression of postsynaptic density protein known as PSD-95 [37]. PSD-95 is a scaffolding protein consisting of multiple protein-protein interaction domains - three N-terminal PDZ domains, an SH3 domain and a C-terminal guanyl-ate kinase domain. The first two PDZ domains interact with the NR2 C-terminal tails while the third PDZ domain... 

Barr, F. (1999). A novel rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins. Gurr. Biol. 9, 381-384. 

Borden, K. L., RING fingers and B-boxes zinc-binding protein-protein interaction domains. Biochem Cell Biol, 1998, 76(2-3), 351-8. 

The crystal structure of Cull has been resolved [21] and found to resemble a long stalk connecting two protein-interaction domains at either end of the stalk. 

Skpl serves as an adaptor protein that provides a molecular link between Cull/ Rod and the F-box proteins [4, 5]. The Skpl protein contains two separate protein-interaction domains that are conserved among its family members between species [21]. The N-terminal region of Skpl (- l-70 a.a.) interacts with Cull while the C-terminal half (100-163 a.a.) binds the F-box proteins [21]. The use of Skpl as an adaptor to link the core ubiquitin E3 ligase components of Cull/Rocl with numerous and diverse substrate-targeting subunits, the F-box proteins, represents a strategy to specifically target many proteins for ubiquitination... 

The F-box protein family is the largest substrate-recognition subunit family. It enables the eukaryotic cells to use the SCF E3 machinery to ubiquitinate a large number of diverse protein substrates. So far, over 70 F-box proteins have been identified in the human genome [57, 58]. F-box proteins all share an 40-amino acid F-box motif, which is usually followed by a C-terminal protein-protein interaction domain such as the WD40 repeats j5-propeller (Fbw subfamily) and /eucine-rich repeats (LRRs Fbl subfamily Figure 7.5) [59, 60]. F-box proteins interact with... 

In addition to the well-established and widely distributed ubiquitin-interaction domains described above, there are several other domains with a more limited scope or with binding properties that are just beginning to be uncovered. Two interesting candidates are the NZF and ZnF-UBP/PAZ domains. 

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