2z6g

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|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00020 ARM], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00185 ARM]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2z6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z6g OCA], [http://www.ebi.ac.uk/pdbsum/2z6g PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2z6g RCSB]</span>
}}
}}
'''Crystal Structure of a Full-Length Zebrafish Beta-Catenin'''
'''Crystal Structure of a Full-Length Zebrafish Beta-Catenin'''
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==Overview==
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beta-catenin plays essential roles in cell adhesion and Wnt signaling, while deregulation of beta-catenin is associated with multiple diseases including cancers. Here, we report the crystal structures of full-length zebrafish beta-catenin and a human beta-catenin fragment that contains both the armadillo repeat and the C-terminal domains. Our structures reveal that the N-terminal region of the C-terminal domain, a key component of the C-terminal transactivation domain, forms a long alpha helix that packs on the C-terminal end of the armadillo repeat domain, and thus forms part of the beta-catenin superhelical core. The existence of this helix redefines our view of interactions of beta-catenin with some of its critical partners, including ICAT and Chibby, which may form extensive interactions with this C-terminal domain alpha helix. Our crystallographic and NMR studies also suggest that the unstructured N-terminal and C-terminal tails interact with the ordered armadillo repeat domain in a dynamic and variable manner.
==About this Structure==
==About this Structure==
2Z6G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z6G OCA].
2Z6G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z6G OCA].
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==Reference==
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Crystal Structure of a Full-Length beta-Catenin., Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W, Structure. 2008 Mar;16(3):478-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18334222 18334222]
[[Category: Danio rerio]]
[[Category: Danio rerio]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Liu, J.]]
[[Category: Liu, J.]]
[[Category: Moon, R.]]
[[Category: Moon, R.]]
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[[Category: Takemaru, K I.]]
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[[Category: Takemaru, K.]]
[[Category: Xing, Y.]]
[[Category: Xing, Y.]]
[[Category: Xu, W.]]
[[Category: Xu, W.]]
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[[Category: full-length]]
[[Category: full-length]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:52:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 10:03:17 2008''

Revision as of 08:03, 26 March 2008


PDB ID 2z6g

Drag the structure with the mouse to rotate
, resolution 3.40Å
Domains: ARM, ARM
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of a Full-Length Zebrafish Beta-Catenin


Overview

beta-catenin plays essential roles in cell adhesion and Wnt signaling, while deregulation of beta-catenin is associated with multiple diseases including cancers. Here, we report the crystal structures of full-length zebrafish beta-catenin and a human beta-catenin fragment that contains both the armadillo repeat and the C-terminal domains. Our structures reveal that the N-terminal region of the C-terminal domain, a key component of the C-terminal transactivation domain, forms a long alpha helix that packs on the C-terminal end of the armadillo repeat domain, and thus forms part of the beta-catenin superhelical core. The existence of this helix redefines our view of interactions of beta-catenin with some of its critical partners, including ICAT and Chibby, which may form extensive interactions with this C-terminal domain alpha helix. Our crystallographic and NMR studies also suggest that the unstructured N-terminal and C-terminal tails interact with the ordered armadillo repeat domain in a dynamic and variable manner.

About this Structure

2Z6G is a Single protein structure of sequence from Danio rerio. Full crystallographic information is available from OCA.

Reference

Crystal Structure of a Full-Length beta-Catenin., Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W, Structure. 2008 Mar;16(3):478-87. PMID:18334222

Page seeded by OCA on Wed Mar 26 10:03:17 2008

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