5WXG
Structure of TAF PHD finger domain binds to H3(1-15)K4ac
Summary for 5WXG
Entry DOI | 10.2210/pdb5wxg/pdb |
Descriptor | Transcription initiation factor TFIID subunit 3, Histone H3K4ac, ZINC ION, ... (5 entities in total) |
Functional Keywords | taf3, histone h3, hydrolase |
Biological source | Homo sapiens (Human) More |
Cellular location | Nucleus : Q5VWG9 |
Total number of polymer chains | 2 |
Total formula weight | 8263.33 |
Authors | |
Primary citation | Zhao, S.,Yang, M.,Zhou, W.,Zhang, B.,Cheng, Z.,Huang, J.,Zhang, M.,Wang, Z.,Wang, R.,Chen, Z.,Zhu, J.,Li, H. Kinetic and high-throughput profiling of epigenetic interactions by 3D-carbene chip-based surface plasmon resonance imaging technology Proc. Natl. Acad. Sci. U.S.A., 114:E7245-E7254, 2017 Cited by PubMed Abstract: Chemical modifications on histones and DNA/RNA constitute a fundamental mechanism for epigenetic regulation. These modifications often function as docking marks to recruit or stabilize cognate "reader" proteins. So far, a platform for quantitative and high-throughput profiling of the epigenetic interactome is urgently needed but still lacking. Here, we report a 3D-carbene chip-based surface plasmon resonance imaging (SPRi) technology for this purpose. The 3D-carbene chip is suitable for immobilizing versatile biomolecules (e.g., peptides, antibody, DNA/RNA) and features low nonspecific binding, random yet function-retaining immobilization, and robustness for reuses. We systematically profiled binding kinetics of 1,000 histone "reader-mark" pairs on a single 3D-carbene chip and validated two recognition events by calorimetric and structural studies. Notably, a discovery on H3K4me3 recognition by the DNA mismatch repair protein MSH6 in suggests a mechanism of H3K4me3-mediated DNA damage repair in plant. PubMed: 28808021DOI: 10.1073/pnas.1704155114 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.703 Å) |
Structure validation
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