9WV4
Crystal structure of human ZMYND8 MYND domain
Summary for 9WV4
| Entry DOI | 10.2210/pdb9wv4/pdb |
| Descriptor | MYND-type zinc finger-containing chromatin reader ZMYND8, ZINC ION, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | zmynd8, mynd domain, metal binding protein, protein -protein interaction domain |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 60693.28 |
| Authors | Srivastava, D.K.,Roy, S. (deposition date: 2025-09-19, release date: 2025-10-08, Last modification date: 2026-08-12) |
| Primary citation | Srivastava, D.K.,Nandi, S.,Karmakar, A.,Das, C.,Roy, S. The chromatin reader ZMYND8 recruits the NuRD component GATAD2A through its MYND domain to regulate MAPT213 long noncoding RNA transcription. J.Biol.Chem., 302:111463-111463, 2026 Cited by PubMed Abstract: The zinc finger MYND-type containing eight protein (ZMYND8) is a chromatin reader that regulates neuronal gene expression by controlling the microtubule-associated protein tau (MAPT) locus. Here, we investigate how ZMYND8 regulates expression of the long non-coding RNA MAPT213 through its interaction with GATA zinc finger domain containing 2A (GATAD2A), a component of the Nucleosome Remodelling and Deacetylase complex. ZMYND8 exhibits opposite regulatory effects on protein-coding MAPT and non-coding MAPT213 transcripts in a manner dependent on its MYND domain, promoting MAPT expression while suppressing MAPT213 levels. Chromatin immunoprecipitation experiments demonstrated that ZMYND8 specifically recruits GATAD2A to the MAPT213 internal regulatory region, establishing a direct link between protein binding and transcriptional control. We determined the crystal structure of the ZMYND8 coiled-coil MYND domain at high resolution, revealing a homodimeric architecture. The MYND domain specifically recognizes GATAD2A through direct interaction with proline-rich motifs in GATAD2A's central region. Structure-function analysis identified critical binding interface residues, while quantitative measurements revealed moderate-affinity interactions enhanced through multivalent binding mechanisms. These findings establish the molecular basis for ZMYND8-mediated recruitment of chromatin remodeling complexes to specific genomic loci and provide a structural framework for understanding transcriptional regulation of MAPT213. PubMed: 41999894DOI: 10.1016/j.jbc.2026.111463 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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