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4p9t

From Proteopedia

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Structure 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4p9t"

Categories: Large Structures | Mus musculus | Hakoshima T | Hirano Y | Shibahara T

@@ Line 1: / Line 1: @@
 ==Structure of the free form of the N-terminal VH1 domain of monomeric alpha-catenin==
-<StructureSection load='4p9t' size='340' side='right' caption='[[4p9t]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='4p9t' size='340' side='right'caption='[[4p9t]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4p9t]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P9T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4p9t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P9T FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p9t OCA], [http://pdbe.org/4p9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p9t RCSB], [http://www.ebi.ac.uk/pdbsum/4p9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p9t ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4p9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p9t OCA], [https://pdbe.org/4p9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p9t RCSB], [https://www.ebi.ac.uk/pdbsum/4p9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p9t ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CTNA2_MOUSE 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.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref>
+[https://www.uniprot.org/uniprot/CTNA2_MOUSE 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.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 21: @@
 ==See Also==
-*[[Catenin|Catenin]]
+*[[Catenin 3D structures|Catenin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Hakoshima, T]]
+[[Category: Large Structures]]
-[[Category: Hirano, Y]]
+[[Category: Mus musculus]]
-[[Category: Shibahara, T]]
+[[Category: Hakoshima T]]
-[[Category: Adherens junction]]
+[[Category: Hirano Y]]
-[[Category: Cytoskeletal protein]]
+[[Category: Shibahara T]]
-[[Category: Helix bundle]]

4p9t

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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