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Structure of the free form of the N‐terminal VH1 domain of monomeric α‐catenin
Author(s) -
Shibahara Takenori,
Hirano Yoshinori,
Hakoshima Toshio
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.05.053
Subject(s) - monomer , chemistry , residue (chemistry) , terminal (telecommunication) , vinculin , domain (mathematical analysis) , stereochemistry , biochemistry , cell , cell adhesion , polymer , telecommunications , mathematical analysis , mathematics , organic chemistry , computer science
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.