5y5w

Crystal structure of human Spindlin1 in complex with a histone H4K20(me3) peptide

spinqualitylabelsall models 5y5w, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5y5w is a 7 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.3Å Ligands: M3L Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SPIN1_HUMAN May play a role in cell-cycle regulation during the transition from gamete to embryo (By similarity). Publication Abstract from PubMed Using methods combining cross-linking, pull-down assays, and stable isotope labeling by amino acids in cell culture with mass spectrometry, we identified that the Tudor domain-containing protein Spindlin-1 recognizes trimethylation of histone H4 lysine 20 (H4K20me3). The binding affinity of Spindlin-1 to H4K20me3 is weaker than that to H3K4me3, indicating H4K20me3 as a secondary substrate for Spindlin-1. Structural studies of Spindlin-1 in complex with the H4K20me3 peptide indicate that Spindlin-1 attains a distinct binding mode for H4K20me3 recognition. Further biochemical analysis identified that Spindlin-1 also binds methylated R23 of H4, providing new clues for the function of Spindlin-1. Spindlin-1 recognizes methylations of K20 and R23 of histone H4 tail.,Wang C, Zhan L, Wu M, Ma R, Yao J, Xiong Y, Pan Y, Guan S, Zhang X, Zang J FEBS Lett. 2018 Dec;592(24):4098-4110. doi: 10.1002/1873-3468.13281. Epub 2018, Nov 17. PMID:30381828 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Spindlin

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