期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 17, 期 3, 页码 348-U121出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1784
关键词
-
资金
- US National Institutes of Health [R01 GM062270, R01 GM30518, U54 CA121852]
- US National Science Foundation [MCB-0416708]
- Biotechnology and Biological Sciences Research Council [BBS/B/06512] Funding Source: researchfish
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [918535] Funding Source: National Science Foundation
Crystal structures of classical cadherins have revealed two dimeric configurations. In the first, N-terminal beta-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 beta-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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据