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Laminin binding domain

Functional domains Transmembrane domain aa 86-101 (Castronovo etal, 1991b), Laminin binding domain aa 161-180 (Castronovo etal., 1991b) PrP = binding domain aa 157 and 180 (Rieger et al, 1997)... [Pg.239]

Fragment 3 (Mr 50K) possessed / structure, appeared globular in electron micrographs, and was found to bind to heparin. It was assumed to be the globular region at the end of the long arm of laminin. This site is one of the main heparin- and heparan sulfate-binding domains in laminin (Ott et al., 1982). [Pg.25]

A FIGURE 6-16 Laminin, a heterotrimeric multiadhesive matrix protein found in all basal laminae, (a) Schematic model showing the general shape, location of globular domains, and coiled-coil region in which laminin s three chains are covalently linked by several disulfide bonds. Different regions of laminin bind to cell-surface receptors and various matrix components. [Pg.213]

R.P Mecham, L. Whitehouse, M. Hay, A. Hinek, M.P. Sheetz, Ligand affinity of the 67-kD elastin/laminin binding protein is modulated by the protein s lectin domain visualization of elastin/ laminin-receptor complexes with gold-tagged ligands, J. Cell Biol. 113 (1991) 187-194. [Pg.57]

Fibronectin is an adhesion protein like laminin, vitronectin, and von Wille-brand factor, which are synthesized by the cells themselves to build up the ECM. The glycoprotein fibronectin with a molecular weight between 220,000 and 250,000 consists of two similar subunits, which are connected close to their C-terminus by disulfide bridges. The subunits are composed of functional domains [121]. The cell binding domain with the characteristic sequence Gly-Arg-Gly-Asp-Ser (GRGDS) is of special interest [122]. Models of the subunit of the fibronectin molecule and its cell binding domain are presented in Fig. 21. [Pg.32]

Several nonconventional cadherins that contain cadherin repeats have been described but they have specific features not found in the classical cadherins [1]. The cadherin Flamingo, originally detected in Drosophila, contains seven transmembrane segments and in this respect resembles G protein-coupled receptors. The extracellular domain of Flamingo and its mammalian homologs is composed of cadherin repeats as well as EGF-like and laminin motifs. The seven transmembrane span cadherins have a role in homotypic cell interactions and in the establishment of cell polarity. The FAT-related cadherins are characterized by a large number of cadherin repeats (34 in FAT and 27 in dachsous). Their cytoplasmic domains can bind to catenins. T- (=truncated-)cadherin differs from other cadherins in that it has no transmembrane domain but is attached to the cell membrane via a glycosylpho-sphatidylinositol anchor. [Pg.307]

The NCI domain of type VII collagen binds to the /33 chain of laminin, " laminin-5 a3(33 2), and type IV collagen. The triple helical domain of type VII collagen functions to promote the migration of human keratinocytes. °... [Pg.488]

While one end of the dystrophin molecule binds to actin filaments, the C-terminal domain associates with several additional proteins to form a dystrophin-glycoprotein complex (see figure)/1 k Dystrophin is linked directly to the membrane-spanning protein P-dystroglycan, which in the outer membrane surfaces associates with a glycoprotein a-dystroglycan. The latter binds to laminin-2 (Fig. 8-33), a protein that binds the cell to the basal lamina. Four... [Pg.1112]

Hoffman MP, Nomizu M, Roque E et al. Laminin-1 and laminin-2 G-domain synthetic peptides bind syndecan-1 and are involved in acinar formation of a human submandibular gland cell line. J Biol Chem 1998 273 28633. [Pg.62]


See other pages where Laminin binding domain is mentioned: [Pg.51]    [Pg.237]    [Pg.238]    [Pg.107]    [Pg.51]    [Pg.237]    [Pg.238]    [Pg.107]    [Pg.137]    [Pg.317]    [Pg.430]    [Pg.473]    [Pg.149]    [Pg.38]    [Pg.205]    [Pg.74]    [Pg.47]    [Pg.68]    [Pg.152]    [Pg.188]    [Pg.204]    [Pg.538]    [Pg.540]    [Pg.541]    [Pg.238]    [Pg.905]    [Pg.47]    [Pg.616]    [Pg.207]    [Pg.170]    [Pg.41]    [Pg.80]    [Pg.185]    [Pg.365]    [Pg.203]    [Pg.1809]    [Pg.1810]    [Pg.651]    [Pg.846]    [Pg.540]    [Pg.490]    [Pg.186]    [Pg.409]    [Pg.1884]    [Pg.187]   
See also in sourсe #XX -- [ Pg.107 ]




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