4P9T

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

Summary for 4P9T

• Entry DOI: 10.2210/pdb4p9t/pdb
• Descriptor: Catenin alpha-2, IODIDE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: cytoskeletal protein, adherens junction, helix bundle, cell adhesion
• Biological source: Mus musculus (Mouse)
• Cellular location: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q61301
• Total number of polymer chains: 4
• Total formula weight: 119340.33

Authors

Shibahara, T.,Hirano, Y.,Hakoshima, T. (deposition date: 2014-04-04, release date: 2015-04-29, Last modification date: 2023-09-27)

Primary citation

Shibahara, T.,Hirano, Y.,Hakoshima, T.
Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin.
Febs Lett., 589:1754-1760, 2015

PubMed 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.

PubMed: 26071377
DOI: 10.1016/j.febslet.2015.05.053

Experimental method

X-RAY DIFFRACTION (2.5 Å)