ArticleCellular and molecular bioengineering2021
Stabilization of the Hinge Region of Human E-selectin Enhances Binding Affinity to Ligands Under Force.
Article in Cellular and molecular bioengineering, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
introductionE-selectin is a member of the selectin family of cell adhesion molecules expressed on the plasma membrane of inflamed endothelium and facilitates initial leukocyte tethering and subsequent cell rolling during the early stages of the inflammatory response
methodsUsing molecular dynamics (MD) simulations we observed that in the absence of tensile force E-selectin undergoes spontaneous switching between the two conformational states at equilibrium. A single amino acid substitution at residue 2 (serine to tyrosine) on the lectin domain favors the extended conformation.
resultsSteered molecular dynamics (SMD) simulations of E-selectin and PSGL-1 in conjunction with experimental cell adhesion assays show a longer binding lifetime of E-selectin (S2Y) to PSGL-1 compared to wildtype protein.
conclusionsThe findings in this study advance our understanding into how the structural makeup of E-selectin allosterically influences its adhesive dynamics.
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