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5TBN

Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide

Summary for 5TBN
Entry DOI10.2210/pdb5tbn/pdb
NMR InformationBMRB: 30177
DescriptorPHD finger protein 20, Histone H3.1, ZINC ION (3 entities in total)
Functional Keywordsphd finger, methylated lysine, transcription - structural protein complex, transcription / structural protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight8242.01
Authors
Cui, G.,Botuyan, M.V.,Mer, G. (deposition date: 2016-09-12, release date: 2016-10-12, Last modification date: 2019-12-04)
Primary citationKlein, B.J.,Wang, X.,Cui, G.,Yuan, C.,Botuyan, M.V.,Lin, K.,Lu, Y.,Wang, X.,Zhao, Y.,Bruns, C.J.,Mer, G.,Shi, X.,Kutateladze, T.G.
PHF20 Readers Link Methylation of Histone H3K4 and p53 with H4K16 Acetylation.
Cell Rep, 17:1158-1170, 2016
Cited by
PubMed Abstract: PHF20 is a core component of the lysine acetyltransferase complex MOF (male absent on the first)-NSL (non-specific lethal) that generates the major epigenetic mark H4K16ac and is necessary for transcriptional regulation and DNA repair. The role of PHF20 in the complex remains elusive. Here, we report on functional coupling between methylation readers in PHF20. We show that the plant homeodomain (PHD) finger of PHF20 recognizes dimethylated lysine 4 of histone H3 (H3K4me2) and represents an example of a native reader that selects for this modification. Biochemical and structural analyses help to explain this selectivity and the preference of Tudor2, another reader in PHF20, for dimethylated p53. Binding of the PHD finger to H3K4me2 is required for histone acetylation, accumulation of PHF20 at target genes, and transcriptional activation. Together, our findings establish a unique PHF20-mediated link between MOF histone acetyltransferase (HAT), p53, and H3K4me2, and suggest a model for rapid spreading of H4K16ac-enriched open chromatin.
PubMed: 27760318
DOI: 10.1016/j.celrep.2016.09.056
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

數據於2024-10-30公開中

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