title: Structure of the free form of the N-terminal VH1 domain of monomeric α-catenin.
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.
authors.affiliation: Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
authors.forename: Takenori
authors.initials: T
authors.lastname: Shibahara
authors.affiliation: Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
authors.forename: Yoshinori
authors.initials: Y
authors.lastname: Hirano
authors.affiliation: Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan. Electronic address: hakosima@bs.naist.jp.
authors.forename: Toshio
authors.initials: T
authors.lastname: Hakoshima
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation; D051178:alpha Catenin / Q000737:chemistry*
chemical_list: D051178:alpha Catenin
keywords: Adherens junction; Conformational switch; Helix bundle; α-Catenin; β-Catenin