1v18: Difference between revisions
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[[Image:1v18.png|left|200px]] | [[Image:1v18.png|left|200px]] | ||
{{STRUCTURE_1v18| PDB=1v18 | SCENE= }} | {{STRUCTURE_1v18| PDB=1v18 | SCENE= }} | ||
===THE CRYSTAL STRUCTURE OF BETA-CATENIN ARMADILLO REPEAT COMPLEXED WITH A PHOSPHORYLATED APC 20MER REPEAT.=== | ===THE CRYSTAL STRUCTURE OF BETA-CATENIN ARMADILLO REPEAT COMPLEXED WITH A PHOSPHORYLATED APC 20MER REPEAT.=== | ||
{{ABSTRACT_PUBMED_15327768}} | {{ABSTRACT_PUBMED_15327768}} | ||
==About this Structure== | ==About this Structure== | ||
[[1v18]] is a 2 chain structure of [[Catenin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V18 OCA]. | |||
==See Also== | |||
*[[Catenin|Catenin]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:015327768</ref><references group="xtra"/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: Beta-catenin degradation complex]] | [[Category: Beta-catenin degradation complex]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Signaling protein]] | |||
[[Category: Signalling complex]] | |||
[[Category: Transcription]] | [[Category: Transcription]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
[[Category: Wnt signal]] | [[Category: Wnt signal]] | ||
Revision as of 22:31, 25 July 2012
THE CRYSTAL STRUCTURE OF BETA-CATENIN ARMADILLO REPEAT COMPLEXED WITH A PHOSPHORYLATED APC 20MER REPEAT.
Template:ABSTRACT PUBMED 15327768
About this Structure
1v18 is a 2 chain structure of Catenin with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
See Also
Reference
- Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. Mol Cell. 2004 Aug 27;15(4):511-21. PMID:15327768 doi:10.1016/j.molcel.2004.08.010