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| [[Image:2vpd.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2vpd.png|left|200px]] |
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| {{STRUCTURE_2vpd| PDB=2vpd | SCENE= }} | | {{STRUCTURE_2vpd| PDB=2vpd | SCENE= }} |
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| '''DECODING OF METHYLATED HISTONE H3 TAIL BY THE PYGO-BCL9 WNT SIGNALING COMPLEX'''
| | ===DECODING OF METHYLATED HISTONE H3 TAIL BY THE PYGO-BCL9 WNT SIGNALING COMPLEX=== |
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| ==Overview==
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| Pygo and BCL9/Legless transduce the Wnt signal by promoting the transcriptional activity of beta-catenin/Armadillo in normal and malignant cells. We show that human and Drosophila Pygo PHD fingers associate with their cognate HD1 domains from BCL9/Legless to bind specifically to the histone H3 tail methylated at lysine 4 (H3K4me). The crystal structures of ternary complexes between PHD, HD1, and two different H3K4me peptides reveal a unique mode of histone tail recognition: efficient histone binding requires HD1 association, and the PHD-HD1 complex binds preferentially to H3K4me2 while displaying insensitivity to methylation of H3R2. Therefore, this is a prime example of histone tail binding by a PHD finger (of Pygo) being modulated by a cofactor (BCL9/Legless). Rescue experiments in Drosophila indicate that Wnt signaling outputs depend on histone decoding. The specificity of this process provided by the Pygo-BCL9/Legless complex suggests that this complex facilitates an early step in the transition from gene silence to Wnt-induced transcription.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18498752}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18498752 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18498752}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zinc]] | | [[Category: Zinc]] |
| [[Category: Zinc-finger]] | | [[Category: Zinc-finger]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:05:27 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:48:29 2008'' |