AI Article Synopsis
- * Researchers used all-atom molecular modeling to analyze the structure and dynamics of glypican-1, HS chains, membranes, and ions, finding that glypican-1's core is stable but can move flexibly due to its long C-terminal region.
- * The study highlights the HS chains' structural variability based on sulfation levels and their ability to interact with nearby molecules, marking an initial step in understanding the glycocalyx and its role in growth factor-receptor interactions.
Article Abstract
Glypican-1 and its heparan sulfate (HS) chains play important roles in modulating many biological processes including growth factor signaling. Glypican-1 is bound to a membrane surface via a glycosylphosphatidylinositol (GPI)-anchor. In this study, we used all-atom molecular modeling and simulation to explore the structure, dynamics, and interactions of GPI-anchored glypican-1, three HS chains, membranes, and ions. The folded glypican-1 core structure is stable, but has substantial degrees of freedom in terms of movement and orientation with respect to the membrane due to the long unstructured C-terminal region linking the core to the GPI-anchor. With unique structural features depending on the extent of sulfation, high flexibility of HS chains can promote multi-site interactions with surrounding molecules near and above the membrane. This study is a first step toward all-atom molecular modeling and simulation of the glycocalyx, as well as its modulation of interactions between growth factors and their receptors.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8176774 | PMC |
| http://dx.doi.org/10.1093/glycob/cwaa092 | DOI Listing |
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