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Lipid-binding domain

To demonstrate an application of TIRF-FLIM, a FRET study of annexin A4 translocation and self-aggregation near the plasma membrane is shown in Fig. 9.4. This is a particularly useful application of TIRF-FLIM, since TIRF provides the spatial contrast of detecting only molecules immediately adjacent to the plasma membrane and the lifetime contrast reports on the aggregation state of annexin A4. Annexins are calcium-dependent lipid-binding domains with a different type of lipid binding domain compared to the common C2 domains (e.g., found in protein kinase C). Annex-ins consist of an N-terminal domain and a core domain binding calcium and phospholipids. The core domain is conserved in the... [Pg.415]

DiNitto, J. P., Cronin, T. C. and Lambright, D. G. Membrane recognition and targeting by lipid-binding domains. Sci. STKE 2003 rel6, 2003. [Pg.360]

Welters, R Takegawa, K. Emr, S.D. Chrispeels, M.J. AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid binding domain. Proc. Natl. Acad. Sci. USA, 91, 11398-11402 (1994)... [Pg.191]

MSP1 (200 residue lipid-binding domain of human apolipoprotein Al)90 PEG precipitate of nanodiscs 0.3-0.5 ppm 263 K gas 283 K sample Signals broaden at lower temperatures... [Pg.143]

Patellin is a newly identified PI binding protein. Patellin 1 (PATL1) is one of a family of six Arabidopsis proteins containing a Sec 14 lipid binding domain... [Pg.184]

Figure 4. Linear representation of the Arabidopsis PIPKs and PLCs. The Arabidopsis PtdlnsP 5-kinases are most similar to the human type I PtdlnsP 5-kinases. There are 11 putative type I /I/PtdlnsP 5-kinases in Arabidopsis arranged in two subfamilies based on size. Subfamily B contains X/PIPK1-9, all of which contain membrane occupation and recognition nexus (MORN) repeats. /1/PIPK10-11 are in Subfamily A with molecular weights less than that of the members of subfamily B and contain no MORN repeats. The Arabidopsis phosphoinositide specific phospholipase C family is most similar to the animal PLC . There are seven functional PI-PLCs in Arabidopisis (Hunt et al., 2004). All isoforms contain EF-hand motifs, the X and Y catalytic domains characteristic of PI-PLCs and a C2 lipid-binding domain. Figure 4. Linear representation of the Arabidopsis PIPKs and PLCs. The Arabidopsis PtdlnsP 5-kinases are most similar to the human type I PtdlnsP 5-kinases. There are 11 putative type I /I/PtdlnsP 5-kinases in Arabidopsis arranged in two subfamilies based on size. Subfamily B contains X/PIPK1-9, all of which contain membrane occupation and recognition nexus (MORN) repeats. /1/PIPK10-11 are in Subfamily A with molecular weights less than that of the members of subfamily B and contain no MORN repeats. The Arabidopsis phosphoinositide specific phospholipase C family is most similar to the animal PLC . There are seven functional PI-PLCs in Arabidopisis (Hunt et al., 2004). All isoforms contain EF-hand motifs, the X and Y catalytic domains characteristic of PI-PLCs and a C2 lipid-binding domain.
Pouting CP, Aravind L. START a lipid-binding domain in StAR, HD-ZIP and signalling proteins. Trends Biochem. Sci. 1999 24 130-132. [Pg.1328]

The receptor-binding domain of apoE has been localized to the region encompassing residues 130-160, and the major lipid-binding domain resides in the carboxyl-terminal one-third of the polypeptide chain (Rail... [Pg.358]

In prokaryotic cells, the protein structural features defining lipid-binding domains are less well conserved than in eukaryotes, and the membrane ligand appears to be an anionic lipid-rich domain with little selectivity for the chemical species of lipid. DnaA (K. Boeneman, 2005), MinD [20], and SecA (Section 5.3) are amphitropic proteins in... [Pg.25]

Georgieva ER, Ramlall TF, Borbat PP, Freed JH, Eliezer D (2010) The lipid-binding domain of wild type and mutant alpha-synuclein compactness and interconversation between the broken and extended helix forms. J Biol Chem 285 28261-28274... [Pg.120]

Erato Doi 32 243583 C2 domain — Calcium lipid binding domain IPR000008 calcium is important for e.g., [55]... [Pg.31]

Steenaart, N.A.E., Silvius, J.R. Shore, G.C. (1996) Biochemistry, 35, 3764-3771. An amphiphilic lipid-binding domain influences the topology of a signal-anchor sequence in the mitochondrial outer membrane. [Pg.17]

CaLB Calcium-dependent lipid binding domain... [Pg.65]

Sudhahar CO, Haney RM, Xue Y, Stahelin RV (2008) Cellular membranes and lipid-binding domains as attractive targets fw drag development. Curr Drag Targets 9 603-613... [Pg.111]


See other pages where Lipid-binding domain is mentioned: [Pg.25]    [Pg.358]    [Pg.102]    [Pg.185]    [Pg.209]    [Pg.765]    [Pg.337]    [Pg.359]    [Pg.359]    [Pg.127]    [Pg.164]    [Pg.105]    [Pg.108]    [Pg.221]    [Pg.227]    [Pg.54]    [Pg.53]    [Pg.53]    [Pg.175]   
See also in sourсe #XX -- [ Pg.127 , Pg.140 ]




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Phosphoinositides protein lipid-binding domains

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