4p9t

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

Structural highlights

4p9t is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CTNA2_MOUSE May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The N-terminal vinculin-homology 1 (VH1) domain of alpha-catenin facilitates two exclusive forms, a monomeric form directly bound to beta-catenin for linking E-cadherin to F-actin or a homodimer for the inhibition of beta-catenin binding. Competition of these two forms is affected by approximately 80 N-terminal residues, whose structure is poorly understood. We have determined the structure of the monomeric free form of the alphaN-catenin VH1 domain and revealed that the N-terminal residues form alpha1 and alpha2 helices to complete formation of the N-terminal four-helix bundle. Dynamic conformational changes of these two helices control formation of the beta-catenin-bound monomer or unbound homodimer.

Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin.,Shibahara T, Hirano Y, Hakoshima T FEBS Lett. 2015 Jul 8;589(15):1754-60. doi: 10.1016/j.febslet.2015.05.053. Epub, 2015 Jun 9. PMID:26071377^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Park C, Falls W, Finger JH, Longo-Guess CM, Ackerman SL. Deletion in Catna2, encoding alpha N-catenin, causes cerebellar and hippocampal lamination defects and impaired startle modulation. Nat Genet. 2002 Jul;31(3):279-84. Epub 2002 Jun 24. PMID:12089526 doi:10.1038/ng908
↑ Togashi H, Abe K, Mizoguchi A, Takaoka K, Chisaka O, Takeichi M. Cadherin regulates dendritic spine morphogenesis. Neuron. 2002 Jul 3;35(1):77-89. PMID:12123610
↑ Abe K, Chisaka O, Van Roy F, Takeichi M. Stability of dendritic spines and synaptic contacts is controlled by alpha N-catenin. Nat Neurosci. 2004 Apr;7(4):357-63. Epub 2004 Mar 21. PMID:15034585 doi:10.1038/nn1212
↑ Shibahara T, Hirano Y, Hakoshima T. Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin. FEBS Lett. 2015 Jul 8;589(15):1754-60. doi: 10.1016/j.febslet.2015.05.053. Epub, 2015 Jun 9. PMID:26071377 doi:http://dx.doi.org/10.1016/j.febslet.2015.05.053

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OCA

[1] Park C, Falls W, Finger JH, Longo-Guess CM, Ackerman SL. Deletion in Catna2, encoding alpha N-catenin, causes cerebellar and hippocampal lamination defects and impaired startle modulation. Nat Genet. 2002 Jul;31(3):279-84. Epub 2002 Jun 24. PMID:12089526 doi:10.1038/ng908

[2] Togashi H, Abe K, Mizoguchi A, Takaoka K, Chisaka O, Takeichi M. Cadherin regulates dendritic spine morphogenesis. Neuron. 2002 Jul 3;35(1):77-89. PMID:12123610

[3] Abe K, Chisaka O, Van Roy F, Takeichi M. Stability of dendritic spines and synaptic contacts is controlled by alpha N-catenin. Nat Neurosci. 2004 Apr;7(4):357-63. Epub 2004 Mar 21. PMID:15034585 doi:10.1038/nn1212

[4] Shibahara T, Hirano Y, Hakoshima T. Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin. FEBS Lett. 2015 Jul 8;589(15):1754-60. doi: 10.1016/j.febslet.2015.05.053. Epub, 2015 Jun 9. PMID:26071377 doi:http://dx.doi.org/10.1016/j.febslet.2015.05.053

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