We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Two-step adhesive binding by classical cadherins.
- Authors
Harrison, Oliver J.; Bahna, Fabiana; Katsamba, Phini S.; Xiangshu Jin; Brasch, Julia; Vendome, Jeremie; Ahlsen, Goran; Carroll, Kilpatrick J.; Price, Stephen R.; Honig, Barry; Shapiro, Lawrence
- Abstract
Crystal structures of classical cadherins have revealed two dimeric configurations. In the first, N-terminal β-strands of EC1 domains 'swap' between partner molecules. The second configuration (the 'X dimer'), also observed for T-cadherin, is mediated by residues near the EC1-EC2 calcium binding sites, and N-terminal β-strands of partner EC1 domains, though held adjacent, do not swap. Here we show that strand-swapping mutants of type I and II classical cadherins form X dimers. Mutant cadherins impaired for X-dimer formation show no binding in short–time frame surface plasmon resonance assays, but in long–time frame experiments, they have homophilic binding affinities close to that of wild type. Further experiments show that exchange between monomers and dimers is slowed in these mutants. These results reconcile apparently disparate results from prior structural studies and suggest that X dimers are binding intermediates that facilitate the formation of strand-swapped dimers.
- Subjects
CADHERINS; CELL adhesion molecules; GLYCOPROTEINS; SURFACE plasmon resonance; DIMERS
- Publication
Nature Structural & Molecular Biology, 2010, Vol 17, Issue 3, p348
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.1784