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Membrane binding domain

The cyclooxygenase active site lies at the end of a long, narrow, hydrophobic tunnel or channel. Three of the u-helices of the membrane-binding domain lie at the entrance to this tunnel. The... [Pg.834]

Hurley, J. H. and S. Misra, Signaling and subcellular targeting by membrane-binding domains. Anna Rev Biophys Biomol Struct, 2000, 29,... [Pg.89]

Verdaguer, N., Corbalan-Garcia, S., Ochoa, W.E., Eita, 1., and Gomez-Eemandez, J.C., 1999, bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine. EMBO J. 18 6329-6338. [Pg.77]

Fig. 15. (A) Schematic presentation of the S-layer glycoprotein of Halobacterium halobium, showing the different glycosylation sites and the membrane binding domain at the C-terminal end. Numbering indicates amino acid positions. (B) Schematic presentation of the three different glycoconjugates (BIBS). From ref. [117]. Fig. 15. (A) Schematic presentation of the S-layer glycoprotein of Halobacterium halobium, showing the different glycosylation sites and the membrane binding domain at the C-terminal end. Numbering indicates amino acid positions. (B) Schematic presentation of the three different glycoconjugates (BIBS). From ref. [117].
Michaely P, Bennett V 1993 The membrane-binding domain of ankyrin contains four independently folded subdomains, each comprised of six ankyrin repeats. J Biol Chem 268 22703-22709... [Pg.137]

Yamane, H. K., Farnsworth, C. C., Xie, H Evans, T Gelb, M. H., Glomset, J. A., Clarke, S Fung, B. K.-K. (1991). Membrane-binding domain of the small G protein G25K contains an S-(all-rrans-geranylgeranyl)cysteine methyl ester at its carboxyl terminus. Proc. Natl. Acad. Sci. USA 88, 286-290. [Pg.333]

CPR is composed of two domains an N-terminal membrane-binding domain and a hydrophilic C-terminal catalytic domain. The C-terminal domain can be cleaved from the N-terminal domain by limited proteolysis. The C-terminal domain consists of an FMN-binding section similar to flavodoxin connected by a linker section to an FAD- and NADPH-binding section similar to ferredoxin-NADP" " reductase. The two flavins are only 4 A apart at their 7,8-dimethyl edges, and the planes of the isoalloxazines form an 150° angle (Figure 6), suggesting that electrons are passed directly from one flavin to other." ... [Pg.75]

Two genes (Pcytla and Pcytlb) encode distinct isoforms of CT, a, and p, respectively. The CTa gene spans approximately 26 kb. Exon 1 is untranslated, exon 2 encodes the translation start site and a nuclear localization signal, exons 4-7 encode the catalytic domain, exon 8 encodes the alpha helical membrane-binding domain, and exon 9 encodes... [Pg.220]

Fig. 6. Translocation of CTP phosphocholine cytidylyltransferase (CT) from an inactive soluble form (CTsol) to a membrane-associated activated form (CTm). The reversible interaction of CT with membranes involves the amphipathic helical region lying on the surface of the membrane so that the hydrophilic region interacts with the negatively charged lipid head groups and the hydrophobic side intercalates into the membrane core. N, amino terminal domain C, carboxyl terminal domain M, membrane-binding domain. Figure kindly supplied by Prof. R. Cornell, Simon Fraser University. (See color plate section, plate no. 7.)... Fig. 6. Translocation of CTP phosphocholine cytidylyltransferase (CT) from an inactive soluble form (CTsol) to a membrane-associated activated form (CTm). The reversible interaction of CT with membranes involves the amphipathic helical region lying on the surface of the membrane so that the hydrophilic region interacts with the negatively charged lipid head groups and the hydrophobic side intercalates into the membrane core. N, amino terminal domain C, carboxyl terminal domain M, membrane-binding domain. Figure kindly supplied by Prof. R. Cornell, Simon Fraser University. (See color plate section, plate no. 7.)...
Plate 12. Ribbon diagram of the structure of ovine PGH synthase-1 homodimer interdigitated via its membrane-binding domain (MBD) into the lumenal surface of the endoplasmic reticulum. (See page 340 in this volume.)... [Pg.330]


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See also in sourсe #XX -- [ Pg.37 , Pg.38 ]




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