Cadherins can dimerize via asymmetric interactions.
AFM force measurements
X-dimer
classical cadherins
molecular dynamics
strand-swap dimer
trans interactions
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
07 2022
07 2022
Historique:
revised:
28
04
2022
received:
11
02
2022
accepted:
02
05
2022
pubmed:
10
5
2022
medline:
14
7
2022
entrez:
9
5
2022
Statut:
ppublish
Résumé
Cadherins are essential cell-cell adhesion proteins that interact in two distinct conformations: X-dimers and strand-swap dimers. Both X-dimers and strand-swap dimers are thought to exclusively rely on symmetric sets of interactions between key amino acids on both cadherin binding partners. Here, we use single-molecule atomic force microscopy and computer simulations to show that symmetry in cadherin binding is dispensable and that cadherins can also interact in a novel conformation that asymmetrically incorporates key elements of both strand-swap dimers and X-dimers. Our results clarify the biophysical rules for cadherin binding and demonstrate that cadherins interact in a more diverse range of conformations than previously understood.
Identifiants
pubmed: 35532156
doi: 10.1002/1873-3468.14373
pmc: PMC9829383
mid: NIHMS1859033
doi:
Substances chimiques
Cadherins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
1639-1646Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM121885
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM133880
Pays : United States
Informations de copyright
© 2022 Federation of European Biochemical Societies.
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