5tdr

Set3 PHD finger in complex with histone H3K4me2

spinqualitylabelsall models 5tdr, resolution 1.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tdr is a 2 chain structure with sequence from Homo sapiens and Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.42Å Ligands: MLY, NA, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H31_HUMAN Publication Abstract from PubMed The plant homeodomain (PHD) finger of Set3 binds methylated lysine 4 of histone H3 in vitro and in vivo; however, precise selectivity of this domain has not been fully characterized. Here, we explore the determinants of methyllysine recognition by the PHD fingers of Set3 and its orthologs. We use X-ray crystallographic and spectroscopic approaches to show that the Set3 PHD finger binds di- and trimethylated states of H3K4 with comparable affinities and employs similar molecular mechanisms to form complexes with either mark. Composition of the methyllysine-binding pocket plays an essential role in determining the selectivity of the PHD fingers. The finding that the histone-binding activity is not conserved in the PHD finger of Set4 suggests different functions for the Set3 and Set4 paralogs. Structural Insight into Recognition of Methylated Histone H3K4 by Set3.,Gatchalian J, Ali M, Andrews FH, Zhang Y, Barrett AS, Kutateladze TG J Mol Biol. 2016 Sep 30. pii: S0022-2836(16)30400-4. doi:, 10.1016/j.jmb.2016.09.020. PMID:27697561 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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