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Lectin domain organization

The most common group of fimbrial adhesins of Escherichia coli occurs at the edge of their fimbriae and have a two-domain organization. The most external N-terminal domain is a lectin, whereas the C-terminal pilin connects to the rest of the fimbrius. In Fig. 5, the lectin domains from E. coli adhesins that have been crystallised in complex with a specific glycan sequence are displayed, with the exception of CfaE that was only crystallized in its glycan-free form. PapGII (Pap for pyelonephritis associated pili) is the fimbrial adhesin at the tip of P fimbriae from... [Pg.637]

Kishore U, Eggleton P, Reid K B (1997). Modular organization of carbohydrate recognition domains in animal lectins. Matrix Biol. 15 583-592. [Pg.154]


See other pages where Lectin domain organization is mentioned: [Pg.243]    [Pg.243]    [Pg.416]    [Pg.80]    [Pg.1702]    [Pg.1713]    [Pg.1722]    [Pg.211]    [Pg.142]    [Pg.326]    [Pg.2448]    [Pg.2469]    [Pg.232]    [Pg.240]    [Pg.174]    [Pg.305]    [Pg.315]    [Pg.394]    [Pg.158]    [Pg.24]    [Pg.350]    [Pg.1177]    [Pg.1702]    [Pg.1778]    [Pg.1870]    [Pg.1962]    [Pg.892]    [Pg.191]   
See also in sourсe #XX -- [ Pg.598 ]




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Domain organization

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