Trefoil factor family domains represent highly efficient conformational determinants for N-linked N,N'-di-N-acetyllactosediamine (LacdiNAc) synthesis.

ABSTRACT: The disaccharide N,N'-di-N-acetyllactose diamine (LacdiNAc, GalNAcβ1-4GlcNAcβ) is found in a limited number of extracellular matrix glycoproteins and neuropeptide hormones indicating a protein-specific transfer of GalNAc by the glycosyltransferases β4GalNAc-T3/T4. Whereas previous studies have revealed evidence for peptide determinants as controlling elements in LacdiNAc biosynthesis, we report here on an entirely independent conformational control of GalNAc transfer by single TFF (Trefoil factor) domains as high stringency determinants. Human TFF2 was recombinantly expressed in HEK-293 cells as a wild type full-length probe (TFF2-Fl, containing TFF domains P1 and P2), as single P1 or P2 domain probes, as a series of Cys/Gly mutant forms with aberrant domain structures, and as a double poi

SUBMITTER: Bonar D 

PROVIDER: S-EPMC4207982 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature