7YYE
Orthorombic crystal structure of YTHDF1 YTH domain (G459N mutant) form I
Summary for 7YYE
| Entry DOI | 10.2210/pdb7yye/pdb |
| Descriptor | YTH domain-containing family protein 1, 1,2-ETHANEDIOL, MALONIC ACID, ... (4 entities in total) |
| Functional Keywords | mrna binding and stability, rna binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 93459.01 |
| Authors | Dalle Vedove, A.,Cazzanelli, G.,Lolli, G. (deposition date: 2022-02-17, release date: 2023-03-01, Last modification date: 2024-03-13) |
| Primary citation | Cazzanelli, G.,Dalle Vedove, A.,Spagnolli, G.,Terruzzi, L.,Colasurdo, E.,Boldrini, A.,Patsilinakos, A.,Sturlese, M.,Grottesi, A.,Biasini, E.,Provenzani, A.,Quattrone, A.,Lolli, G. Pliability in the m 6 A-Binding Region Extends Druggability of YTH Domains. J.Chem.Inf.Model., 2024 Cited by PubMed Abstract: Epitranscriptomic mRNA modifications affect gene expression, with their altered balance detected in various cancers. YTHDF proteins contain the YTH reader domain recognizing the mA mark on mRNA and represent valuable drug targets. Crystallographic structures have been determined for all three family members; however, discrepancies are present in the organization of the mA-binding pocket. Here, we present new crystallographic structures of the YTH domain of YTHDF1, accompanied by computational studies, showing that this domain can exist in different stable conformations separated by a significant energetic barrier. During the transition, additional conformations are explored, with peculiar druggable pockets appearing and offering new opportunities for the design of YTH-interfering small molecules. PubMed: 38417111DOI: 10.1021/acs.jcim.4c00051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
