2LHX

Di-O-GalNAc glycosylated Mucin sequence based on MUC2 Mucin glycoprotein tandem repeat

Summary for 2LHX

• Entry DOI: 10.2210/pdb2lhx/pdb
• Related: 2LHV 2LHW 2LHY 2LHZ 2LI0 2LI1 2LI2
• NMR Information: BMRB: 17870
• Descriptor: MUC2 Mucin Domain Peptide, 2-acetamido-2-deoxy-alpha-D-galactopyranose (2 entities in total)
• Functional Keywords: glycosylation, tn antigen, sugar binding protein
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 1224.36

Authors

Borgert, A.,Heimburg-Molinaro, J.,Lasanajak, Y.,Ju, T.,Liu, M.,Thompson, P.,Ragupathi, G.,Barany, G.,Cummings, R.,Smith, D.,Live, D. (deposition date: 2011-08-18, release date: 2012-04-04, Last modification date: 2023-06-14)

Primary citation

Borgert, A.,Heimburg-Molinaro, J.,Song, X.,Lasanajak, Y.,Ju, T.,Liu, M.,Thompson, P.,Ragupathi, G.,Barany, G.,Smith, D.F.,Cummings, R.D.,Live, D.
Deciphering structural elements of mucin glycoprotein recognition.
Acs Chem.Biol., 7:1031-1039, 2012

PubMed Abstract: Mucin glycoproteins present a complex structural landscape arising from the multiplicity of glycosylation patterns afforded by their numerous serine and threonine glycosylation sites, often in clusters, and with variations in respective glycans. To explore the structural complexities in such glycoconjugates, we used NMR to systematically analyze the conformational effects of glycosylation density within a cluster of sites. This allows correlation with molecular recognition through analysis of interactions between these and other glycopeptides, with antibodies, lectins, and sera, using a glycopeptide microarray. Selective antibody interactions with discrete conformational elements, reflecting aspects of the peptide and disposition of GalNAc residues, are observed. Our results help bridge the gap between conformational properties and molecular recognition of these molecules, with implications for their physiological roles. Features of the native mucin motifs impact their relative immunogenicity and are accurately encoded in the antibody binding site, with the conformational integrity being preserved in isolated glycopeptides, as reflected in the antibody binding profile to array components.

PubMed: 22444368
DOI: 10.1021/cb300076s

Experimental method

SOLUTION NMR