C domain

Janin, J., Chothia, C. Domains in proteins definitions, location and structural principles. Methods Enzymol. 115 420-430, 1985. 

Figure 13.31 Space-filling diagram of Src tyrosine kinase in the same view as Figure 13.30. The SH2 domain makes only a few contacts with the rest of the molecule except for the tail region of the kinase. The SH3 domain contacts the N-domain of the kinase in addition to the linker region. There are extensive contacts between the N- and C-domains of the kinase. (Adapted from W. Xu et al., Nature 385 596-602, 1997.)...

The hydrophobic C domain appears to start with an amphipathic membrane-spanning helix [5]. 

Fig. 4. Domain complementation schemes. (A) A domain complementation. The H554A site-directed mutant is inactive in P-enolpyruvate-dependent mannitol phosphorylation because it cannot accept a phosphoryl group from P-FIpr. The measure of A domain activity is its ability to restore mannitol phosphorylation activity to this mutant. A domain activity in the AB subcloned protein can also be measured. (B) B domain complementation. The C384S site-directed mutant is inactive in P-enolpyruvate-dependent mannitol phosphorylation because it cannot pass the phosphoryl group from H554 on its own A domain to mannitol. The measure of B domain activity is its ability to restore mannitol phosphorylation activity to this mutant. B domain activity in the AB subcloned protein can also be measured. (C) C domain complementation. The activity of the C domain is measured by complementation with the purified AB domain.

Chemical modifications like alkylation with (A-ethylmaleimide (NEM) or oxidation with diamide that inhibit the phosphorylation activity of the enzyme did not seem to have any significant effect on the high affinity binding site when the enzyme was solubilized in the detergent decyl-PEG [69,41]. However, in the intact membrane these treatments reduced the affinity by a factor of 2-3. The reduction of the affinity was exclusively due to modification of the cysteine residue at position 384 in the B domain [69]. Apparently, the detergent effects the interaction between the B and C domains. 

Unphosphorylated functioning according to Fig. 5 catalyzes facilitated diffusion of mannitol across the membrane. The same process has been reported for purified II reconstituted in proteoliposomes [70]. The relevance of this activity in terms of transport of mannitol into the bacterial cell is probably low, but it may have important implications for the mechanism by which E-IIs catalyze vectorial phosphorylation. It would indicate that the transmembrane C domain of Il is a mannitol translocating unit which is somehow coupled to the kinase activity of the cytoplasmic domains. We propose that the inwardly oriented binding site which is in contact with the internal water phase (Ecyt Mtl, see Fig. 5) is the site from where mannitol is phosphorylated when transport is coupled to phosphorylation. Meehan-... 

It should be noted that while TE domains represent the most common solution in releasing macrocyclic NRPs and PKs, other pathways are known. For instance, in the biosynthesis of cyclosporine, the cyclization is proposed to be catalyzed by the most downstream C-domain [48]. Macrocyclization can also occur under reduction of a carbonyl group mediated by a reduction domain (R-domain) as proposed in the synthesis of the macrocyclic imine nostocyclopeptide [49]. The synthetic utility of these cyclization strategies has not yet been reported. 

This essential property of IF2 can be tested in at least three different ways, all of which require the availability of f[3H]Met-tRNA and IF2, which are prepared according to the protocol detailed in Milon et al. (2007). However, all the tests described in this section can make use of the sturdier and smaller C domain of Bacillus stearothermophilus IF2, since this domain contains all molecular determinants for the IF2-fMet-tRNA interaction (Guenneugues et al, 2000 Spurio et al, 2000). The method for the preparation and purification of B. stearothermophilus IF2C is essentially that described by Spurio et al. (1993). The concentration of the protein... 

Delle Fratte, S., Piubelli, C., and Domenici, E. (2002). Development of a high-throughput scintillation proximity assay for the identification of C-domain translational initiation factor 2 inhibitors. J. Biomol. Screen. 7, 541—546. 

At 293 K two calcium ions bind cooperatively at the C-domain, with logK = 7.3, 7.6. 

C2, protein kinase C domain ENTH, epsin N-terminal homology FERM, band 4.1,exrin, radixin, moesin FYVE, Fabl, YOTB, Vacl, EEA1 MARCKS, myristoylated alanine-rich protein kinase C substrate PH, pleckstrin homology. 

In another recent example, Hashimoto reported photoaffinity experiments on retinoic acid receptors (RAR). Retinoic acid plays a critical role in cell proliferation and differentiation. RARs belong to the superfamily of nuclear/ thyroid hormone receptors. They consist of six transmembrane domains (A-F) which is a general feature of these receptors. The A/B domains have an autonomous transactivation function while the C-domain contains the Zn-finger, which binds to DNA. The large E-domain participates in ligand binding, dimerization, and ligand dependent transactivation. Finally, D- and F-domains help the orientation and stabilization of the E-domain. 

F. Filament Formation Is Not Based on Interactions Between the N- and C-Domains... 

In those cases where the injection of self-nuclei in every MD is most difficult in view of the very large number of MDs, domain III is split into two domains. Evaluation of the self-nucleation of the PE block within S35E15C50219 shows that not only domain II is absent, but upon decreasing Ts, the PE block is annealed before any detectable self-nucleation occurs (Fig. 17c). Therefore two subdomains were defined [98] domain IIIa, where annealing without previous self-nucleation occurs and domain IIIsa> where self-nucleation and annealing are simultaneously observed for Ts < 88 °C. Domain IIIsa would be the exact equivalent to the standard domain III established by Fillon et al. [75]. 

Figure 4.10 (a) The Cu-Zn superoxide dismutase is made up of eight anti-parallel P-strands both the constant (b) and variable (c) domains of immunoglobulins are made up of seven anti-parallel P-strands with the same topology the variable domain contains two additional P-strands. (From Branden and Tooze, 1991. Reproduced by permission of Garland Publishing, Inc.)... 

B cell bh4 bp BPI BSA C domain C1-C9 cAMP CAP CD cDNA CFU CFU-GEMM bone-marrow-derived lymphocyte tetrahydrobiopterin base pairs bactericidal/permeability-inducing protein bovine serum albumin constant domain complement components cyclic adenosine monophosphate cationic antimicrobial protein cluster of differentiation complementary deoxynucleic acid colony-forming unit granulocyte-erythroid-monocyte-megakaryocyte CFU... 

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