Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10).
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Summary
A chimeric enzyme in which the two domains of pp-GalNAc-T10 acquires activity toward non-glycosylated acceptors, identifying a potential mechanism for generating the various acceptor specificities in different isozymes to produce a wide range of O-glycans.
- Type
- article
- Published
- 2006-06-09
- Cited by
- 111
- References
- 48
- OpenAlex
- https://openalex.org/W16650853
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:34341597
Keywords
Geology
References
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- Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase.
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- Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs
- Crystal Structure of an α1,4-N-Acetylhexosaminyltransferase (EXTL2), a Member of the Exostosin Gene Family Involved in Heparan Sulfate Biosynthesis*
- The structural basis for specificity in human ABO(H) blood group biosynthesis
- Mucin Core O-Glycosylation Is Modulated by Neighboring Residue Glycosylation Status
- Crystallography & NMR system: A new software suite for macromolecular structure determination.
- The CCP4 suite: programs for protein crystallography.
- Isoform-specific O-glycosylation by murine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3, in vivo.
- Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9).
- Role of peptide sequence and neighboring residue glycosylation on the substrate specificity of the uridine 5'-diphosphate-alpha-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyl transferases T1 and T2: kinetic modeling of the porcine and canine submaxillary gland mucin tandem repeats.
- The Lectin Domain of UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase 1 Is Involved in O-Glycosylation of a Polypeptide with Multiple Acceptor Sites*
- A novel human UDP‐N‐acetyl‐D‐galactosamine:polypeptide N‐acetylgalactosaminyltransferase, GalNAc‐T7, with specificity for partial GalNAc‐glycosylated acceptor substrates
- Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module.
- The Lectin Domain of UDP-N-acetyl-d-galactosamine:PolypeptideN-acetylgalactosaminyltransferase-T4 Directs Its Glycopeptide Specificities*
- Glycopeptide N-acetylgalactosaminyltransferase specificities for O-glycosylated sites on MUC5AC mucin motif peptides.
- Substrate-induced conformational changes in glycosyltransferases.
- cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3.
- Cloning and Expression of a Novel, Tissue Specifically Expressed Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family*
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- Function of conserved aromatic residues in the Gal/GalNAc‐glycosyltransferase motif of UDP‐GalNAc:polypeptide N‐acetylgalactosaminyltransferase 1
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- CHARMM Additive All-Atom Force Field for Phosphate and Sulfate Linked to Carbohydrates
- Substrate-induced conformational changes and dynamics of UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase-2.
- Identification of a novel human UDP-GalNAc transferase with unique catalytic activity and expression profile.
- Structure-based Evolutionary Relationship of Glycosyltransferases: A Case Study of Vertebrate β1, 4-Galactosyltransferase, Invertebrate β1,4-N-acetylgalactosaminyltransferase and α-Polypeptidyl-N-acetylgalactosaminyltransferase
- Acceptor specificities and selective inhibition of recombinant human Gal- and GlcNAc-transferases that synthesize core structures 1, 2, 3 and 4 of O-glycans
- Site directed processing: role of amino acid sequences and glycosylation of acceptor glycopeptides in the assembly of extended mucin type O-glycan core 2.
- "Add-on" domains of Drosophila β1,4-N-acetylgalactosaminyltransferase B in the stem region and its pilot protein
- The human collagen beta(1-O)galactosyltransferase, GLT25D1, is a soluble endoplasmic reticulum localized protein
- Crossroads between Bacterial and Mammalian Glycosyltransferases
- The Catalytic and Lectin Domains of UDP-GalNAc:Polypeptide α-N-Acetylgalactosaminyltransferase Function in Concert to Direct Glycosylation Site Selection*
- The Lectin Domain of the Polypeptide GalNAc Transferase Family of Glycosyltransferases (ppGalNAc Ts) Acts as a Switch Directing Glycopeptide Substrate Glycosylation in an N- or C-terminal Direction, Further Controlling Mucin Type O-Glycosylation*
- Site‐Specific Linking of Biomolecules via Glycan Residues Using Glycosyltransferases
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