This work employs large-scale all-atom molecular dynamics simulations to investigate the molecular origin of secondary structure in sulfated GAGs and introduces a two-parameter structural metric that objectively classifies GAG secondary structures and distinguishes heparin helices from related conformations.
Glycosaminoglycans (GAGs) are complex carbohydrates ubiquitously expressed on cell surfaces and within the extracellular matrix, where they regulate essential biological processes through sequence- and sulfation-dependent interactions. Major GAG classes, including heparan sulfate (HS), chondroitin sulfate (CS), dermata...
Jasper S Dumalaog, Shang-Cheng Hung· Current Opinion in Chemical...· 0 citations
Glycosaminoglycan (GAG) polysaccharides play vital roles in animal physiology and disease1. Their diverse and intricate patterns of sulfation and epimerization endow them with an extensive potential to encode functional information2,3. GAG characterization, however, remains a formidable challenge for state-of-the-art e...
Lemuel L. M. Szeto, Anna Yucknovsky, Daniel Cole et al.· bioRxiv· 0 citations
It is concluded that, depending on the 6-O-sulfation pattern and the length of the oligosaccharide, either predominantly electrostatic interactions or a more complex interplay between electrostatic and hydrophobic interactions determines the specificity of the resulting protein-glycosaminoglycan complex.
Sergey A. Samsonov, A. Sieradzan, Avner Yayon· Glycobiology· 0 citations
Together, these studies establish how GAGs are organized in the CXCL8-bound complex and highlight the value of complementary low-resolution structural methods for characterizing GAG-protein complexes.
M. A. White, B. Mahler, Prem Raj B. Joseph et al.· Biochemical Journal· 0 citations
The results provide a molecular-level framework for GAG-assisted maturation of procathepsin K, highlighting cooperative environmental and allosteric regulation of zymogen activation.
Damian Suchomski, P. Wesołowski, K. Bojarski· Biophysical Chemistry· 0 citations
N- and O-glycosylations are essential post-translational modifications involved in numerous physiological and pathological processes. Sulfated N- and O-glycans, commonly found on biologically important glycoproteins, serve as critical mediators of molecular recognition. However, their precise structure-function relatio...
