Receptor interaction domains

Transcription intermediary factor 2, a transcriptional coregulatory protein which contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity... 

Figure 31.24. Coactivator Structure. The pi60 family of coactivators includes a number of domains that can be recognized at the amino acid sequence level, including a basic helix-loop-helix domain that takes part in DNA binding, a PAS domain that participates in protein-protein interactions, a central domain that contacts the ligandbinding domain of the nuclear hormone receptors, and a domain that interacts with additional coactivators such as p300 and CREB-binding protein (CBP). (CREB stands for cyclic AMP-response element binding protein.) The nuclear hormone receptor interaction domain includes three Leu-X-X-Leu-Leu sequences.

Huang N, vom Baur E, Gamier JM, Ler-ouge T, Vonesch JL, et al. 1998. Two distinct nuclear receptor interaction domains in NSD1, a novel SET protein that exhibits characteristics of both corepressors and coactivators.EMBOJ. 17 3398—412... 

The pl60 family of coactivators including steroid receptor coactivator 1 (SRC-1), TIF/GRIP (SRC-2), and ACTR/pCIP (SRC-3) [24] stimulates the transcriptional activity of nuclear receptors. The pi60 family of coactivators has three LXXLL motifs in the receptor-interacting domain (RID) that interacts with the AF-2 domain of nuclear receptors. SRC-1 is a weak HAT that interacts with p300/CBP and recruits CARM-1. 

Figure 13.22 Hormone-receptor interactions involving the domain-domain linker region in the receptor, (a) Interactions between the growth hormone (red) and the growth hormone receptor (blue) linker region. Glu 127 of the receptor forms a salt bridge to Arg 167 in the hormone, (b) The same interaction area in the growth hormone (red)-prolactin receptor (green) complex. The displacement of the linker region due to differences in the domain orientations have brought Asp 124 in the prolactin receptor into contact with Arg 167 of the hormone. (Adapted from W. Somers et al.. Nature 372 478-481, 1994.)...

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. 

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... 

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