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- W4366998122 abstract "Recognition of integrins by CD62P has not been reported and this motivated a docking simulation using integrin αvβ3 as a target. We predicted that the C-type lectin domain of CD62P functions as a potential integrin ligand and observed that it specifically bound to soluble β3 and β1 integrins. Known inhibitors of the interaction between CD62P-PSGL-1 did not suppress the binding, whereas the disintegrin domain of ADAM-15, a known integrin ligand, suppressed recognition by the lectin domain. Furthermore, an R16E/K17E mutation in the predicted integrin-binding interface located outside of the glycan-binding site within the lectin domain, strongly inhibited CD62P binding to integrins. In contrast, the E88D mutation that strongly disrupts glycan binding only slightly affected CD62P-integrin recognition, indicating that the glycan and integrin-binding sites are distinct. Notably, the lectin domain allosterically activated integrins by binding to the allosteric site 2. We conclude that CD62P-integrin binding may function to promote a diverse set of cell-cell adhesive interactions given that β3 and β1 integrins are more widely expressed than PSGL-1 that is limited to leukocytes." @default.
- W4366998122 created "2023-04-27" @default.
- W4366998122 creator A5019384731 @default.
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- W4366998122 date "2023-04-25" @default.
- W4366998122 modified "2023-10-14" @default.
- W4366998122 title "The C-type lectin domain of CD62P (P-selectin) functions as an integrin ligand" @default.
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- W4366998122 doi "https://doi.org/10.26508/lsa.202201747" @default.
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