5VNB
YEATS in complex with histone H3
Summary for 5VNB
| Entry DOI | 10.2210/pdb5vnb/pdb |
| Related | 5VNA |
| Descriptor | YEATS domain-containing protein 4, H3K23acK27ac peptide, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | histone reader, yeats domain, transcription |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 71323.72 |
| Authors | Cho, H.J.,Cierpicki, T. (deposition date: 2017-04-29, release date: 2018-09-05, Last modification date: 2024-10-09) |
| Primary citation | Cho, H.J.,Li, H.,Linhares, B.M.,Kim, E.,Ndoj, J.,Miao, H.,Grembecka, J.,Cierpicki, T. GAS41 Recognizes Diacetylated Histone H3 through a Bivalent Binding Mode. ACS Chem. Biol., 13:2739-2746, 2018 Cited by PubMed Abstract: GAS41 is a chromatin-associated protein that belongs to the YEATS family and is involved in the recognition of acetyl-lysine in histone proteins. A unique feature of GAS41 is the presence of a C-terminal coiled-coil domain, which is responsible for protein dimerization. Here, we characterized the specificity of the GAS41 YEATS domain and found that it preferentially binds to acetylated H3K18 and H3K27 peptides. Interestingly, we found that full-length, dimeric GAS41 binds to diacetylated H3 peptides with an enhanced affinity when compared to those for monoacetylated peptides, through a bivalent binding mode. We determined the crystal structure of the GAS41 YEATS domain with H3K23acK27ac to visualize the molecular basis of diacetylated histone binding. Our results suggest a unique binding mode in which full-length GAS41 is a reader of diacetylated histones. PubMed: 30071723DOI: 10.1021/acschembio.8b00674 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
