5Y5W

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

Summary for 5Y5W

• Entry DOI: 10.2210/pdb5y5w/pdb
• Descriptor: Spindlin-1, Histone peptide H4K20(me3) (2 entities in total)
• Functional Keywords: reader, histone, gene regulation
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 7
• Total formula weight: 111181.88

Authors

Wang, C.,Zang, J. (deposition date: 2017-08-10, release date: 2017-10-11, Last modification date: 2023-11-22)

Primary citation

Wang, C.,Zhan, L.,Wu, M.,Ma, R.,Yao, J.,Xiong, Y.,Pan, Y.,Guan, S.,Zhang, X.,Zang, J.
Spindlin-1 recognizes methylations of K20 and R23 of histone H4 tail
FEBS Lett., 592:4098-4110, 2018

PubMed Abstract: 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.

PubMed: 30381828
DOI: 10.1002/1873-3468.13281

Experimental method

X-RAY DIFFRACTION (3.3 Å)