E box motif

Margottin, F., et al., A novel human WD protein, h-beta TrCp, that interacts with HlV-1 Vpu connects CD4 to the ER degradation pathway through an E-box motif. Mol Cell,... 

Travers, M.T., Vallance, A.J., Gourlay, H.T., Gill, C.A., Klein, I., Bottema, C.B., Barber, M.C. 2001. Promoter I of the ovine acetyl-CoA carboxylase-alpha gene an E-box motif at -114 in the proximal promoter binds upstream stimulatory factor (USF)-l and USF-2 and acts as an insulin-response sequence in differentiating adipocytes. Biochem. J. 359, 273-284. 

Pringa, E., Martinez-Noel, G., Muller, U., and Harbers, K. Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugatmg enzymes. 

By virtue of its helix-loop-helix motif, MyoD is able to form homodimers, as well as heterodimers, with other ubiquitously expressed helix-loop-helix proteins, such as E12 and E47. MyoD-E-protein heterodimers bind to E-box DNA more tightly than MyoD homodimers and act as stronger activators of transcription. MyoD-E47 heterodimers were found to bind to bimolecular G-quadruplex structures more weakly than MyoD homodimers. Specifically, MyoD heterodimers bound more tightly to E-box DNA than to bimolecular G-quadruplex structures of promoter sequences of the sMtCK and ot7 integrin, as reflected by... 

Yoon SO, Chikaraishi DM. Tissue specific transcription of the rat tyrosine hydroxylase gene requires synergy between an AP-1 motif and an overlapping E box-containing dyad. Neuron 1992 9 55-67. 

Hydrophobicity plots of AQPs indicated that these proteins consist of six transmembrane a-helices (Hl-H6 in Fig. la) connected by five connecting loops (A-E), and flanked by cytosolic N- and C-termini. The second half of the molecule is an evolutionary duplicate and inverse orientation of the first half of the molecule. Loops B and E of the channel bend into the membrane with an a-helical conformation (HB, HE in Fig. lb) and meet and each other at their so-called Asn-Pro-Ala (NPA) boxes. These NPA motifs are the hallmark of AQPs and form the actual selective pore of the channel, as at this location, the diameter is of that of a water molecule (3 A Fig. la and b). Based on the narrowing of the channel from both membrane sides to this small... 

A recent study showed that several APC substrates contain a motif comprising threonine (T), glutamate (E), and lyinse (K) residues that has been termed the TEK-box. " A similar TEK-box is also present around Lysl 1 of uhiquitin. The TEK-box is believed to be a new interaction motif critical for recognizing APC substrates for ubiquitination. It is important to note that TEK-box-containing substrates receive a Kll uhiquitin linkage as... 

Fig. 3. Amino acid sequence of several somatic human histone HI proteins to illustrate the microheterogeneity of linker histones. The sequences for human histone HI variants (H1.1-H1.4) were obtained from Ref [373] and Hl-5 was from Ref [412]. The nomenclature followed for the designation of these histone variants was Doenecke (e.g., see Ref. [412]). The nomenclature of Parseghian et at. [373] is shown in parentheses. The regions corresponding to the trypsin-resistant (winged helix motif [96]) which is characteristic of the protein members of the histone HI family are indicated by a boxed inset.

The fact that GBF-1 bound to the cab-E G-box-like sequence, but bound only weakly to the USF recognition sequence and the G-box-like elements of the A. majus chalcone synthase promoter, contrasted with results reported for the plant nuclear factor CG-1 (Staiger et al., 1989). This latter factor was shown to interact with both the USF recognition sequence and one of the G-box-like elements of the A. majus chalcone synthase promoter it did not interact with the cab-E motif. These cumulative DNA-binding studies indicate that GBF-1 and CG-1 have different DNA-binding properties. 

Figure 2 Order and organization of enniatin synthetase and cyclosporin synthetase as deduced from gene sequence and biochemical characterization. Symbols in the adenylateforming modules (black boxes) indicate the corresponding activated amino acids. M stands for A -methyltransferase domain. Condensation domains are represented by white boxes. (A) Top Structure of enniatin synthetase. EA represents the D-Hiv-activating module EB represents the L-valine-activating module D-Ehv is D-2-hydroxyisovaleric acid. Bottom Structural features of the wild-type A -methyltransferase domain M of esynl. The black boxes indicate conserved motifs which can be found within methyltransferases and A -methyltransferase domains of peptide synthetases (see also Fig. 3). The numbers indicate the amino acid position in the sequence of Esyn. (B) Structure of cyclosporin synthetase. Abu = L-a-aminobutyric acid Bmt = (4A)-4-[(E)-2-butenyl]-4-methyl-L-threonine.

Fig. 5. Three-dimensional structures of the (iaPPaP proteins oftheAtxl-like family. MXCXXC motif residues are hoxed. The Protein Data Bank (pdh) code for each structure is in parentheses, (a) NMR structure of Shigella flexneri Hg(II)MerP (Steele and Opella, 1997). (h) X-ray structure oiSaccharamyces cerevisiae Hg(II)Atxl. K24, K28, K59, and K62, side chains important in the recognition of the Ccc2a target domain, are shown outside of the hox (see text) (Rosenzweig et al., 1999). (c) X-ray structure of human Cu(I)Hahl. R21, K25, K56, and K57, side chains important in the recognition of the fourth N-terminal domain of the Menkes protein, are shown outside of the box (Wernimont et al., 2000). (d) NMR structure oi Enterococcus hirae apoCopZ (Wimmer et al., 1999). (e) NMR structure of human Ag(l)Mnk4, the fourth domain of the...

Schneider S, Campodonico E, Schwer B. Motifs IV and V in the DEAH box splicing factor Prp22 are important for RNA unwinding, and helicase-defective Prp22 mutants are suppressed by Prp8. J. Biol. Chem. 2004 279 8617-8626. 

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