Structure, Dynamics, and Interactions of GPI-Anchored Human Glypican-1 with Heparan Sulfates in a Membrane
| Autor: | Yeol Kyo Choi, Linda J. Lowe-Krentz, Göran Widmalm, Wonpil Im, Chuqiao Dong, X. Frank Zhang, Jumin Lee, Aurelia R. Honerkamp-Smith |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Molecular model Glycosylphosphatidylinositols 01 natural sciences Biochemistry Regular Manuscripts Glycocalyx 03 medical and health sciences Molecular dynamics chemistry.chemical_compound Sulfation Glypicans 0103 physical sciences Molecule Humans Glypican-1 030304 developmental biology 0303 health sciences 010304 chemical physics Molecular Structure Chemistry Cell Membrane Computational Biology Heparan sulfate Membrane Biophysics Thermodynamics Heparitin Sulfate |
| Zdroj: | Glycobiology |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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