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FEBS Lett. 2015 Jul 8;589(15):1754-60. doi: 10.1016/j.febslet.2015.05.053. Epub 2015 Jun 9.

Structure of the free form of the N-terminal VH1 domain of monomeric α-catenin.

Author information

1
Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
2
Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan. Electronic address: hakosima@bs.naist.jp.

Abstract

The N-terminal vinculin-homology 1 (VH1) domain of α-catenin facilitates two exclusive forms, a monomeric form directly bound to β-catenin for linking E-cadherin to F-actin or a homodimer for the inhibition of β-catenin binding. Competition of these two forms is affected by ∼80 N-terminal residues, whose structure is poorly understood. We have determined the structure of the monomeric free form of the αN-catenin VH1 domain and revealed that the N-terminal residues form α1 and α2 helices to complete formation of the N-terminal four-helix bundle. Dynamic conformational changes of these two helices control formation of the β-catenin-bound monomer or unbound homodimer.

KEYWORDS:

Adherens junction; Conformational switch; Helix bundle; α-Catenin; β-Catenin

PMID:
26071377
DOI:
10.1016/j.febslet.2015.05.053
[Indexed for MEDLINE]
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