Distinct binding kinetics of E-, P- and L-selectins to CD44.
CD44
binding epitope
binding kinetics
selectin
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
05 2022
05 2022
Historique:
revised:
22
10
2021
received:
17
07
2021
accepted:
26
11
2021
pubmed:
29
11
2021
medline:
20
5
2022
entrez:
28
11
2021
Statut:
ppublish
Résumé
Molecular-level selectin-cluster of differentiation 44 (CD44) interactions are far from clear because of the complexity and diversity of CD44 glycosylation and isoforms expressed on various types of cells. By combining experimental measurements and simulation predictions, the binding kinetics of three selectin members to the recombinant CD44 were quantified and the corresponding microstructural mechanisms were explored, respectively. Experimental results showed that the E-selectin-CD44 interactions mainly mediated the firm adhesion of microbeads under shear flow with the strongest rupture force. P- and L-selectins had similar interaction strength but different association and dissociation rates by mediating stable rolling and transient adhesions of microbeads, respectively. Molecular docking and molecular dynamics (MD) simulations predicted that the binding epitopes of CD44 to selectins are all located at the side face of each selectin, although the interfaces denoted as the hinge region are between lectin and epidermal growth factor domains of E-selectin, Lectin domain side of P-selectin and epidermal growth factor domain side of L-selectin, respectively. The lowest binding free energy, the largest rupture force and the longest lifetime for E-selectin, as well as the comparable values for P- and L-selectins, demonstrated in both equilibration and steered MD simulations, supported the above experimental results. These results offer basic data for understanding the functional differences of selectin-CD44 interactions.
Substances chimiques
E-Selectin
0
Selectins
0
L-Selectin
126880-86-2
Epidermal Growth Factor
62229-50-9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2877-2894Informations de copyright
© 2021 Federation of European Biochemical Societies.
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