3DWH
Structural and Functional Analysis of SRA domain
Summary for 3DWH
| Entry DOI | 10.2210/pdb3dwh/pdb |
| Descriptor | E3 ubiquitin-protein ligase UHRF1, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | beta barrel, cell cycle, dna damage, dna repair, dna-binding, ligase, metal-binding, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation pathway, zinc-finger |
| Biological source | Homo sapiens (Human) |
| Cellular location | Nucleus: Q96T88 |
| Total number of polymer chains | 1 |
| Total formula weight | 23436.09 |
| Authors | Qian, C.,Jakoncic, J.,Zhou, M. (deposition date: 2008-07-22, release date: 2008-10-21, Last modification date: 2024-03-13) |
| Primary citation | Qian, C.,Li, S.,Jakoncic, J.,Zeng, L.,Walsh, M.J.,Zhou, M.M. Structure and Hemimethylated CpG Binding of the SRA Domain from Human UHRF1. J.Biol.Chem., 283:34490-34494, 2008 Cited by PubMed Abstract: Human UHRF1 (ubiquitin-like PHD and RING finger 1) functions to maintain CpG DNA methylation patterns through DNA replication by co-localizing with the DNA methyltransferase DNMT1 at chromatin in mammals. Recent studies show that UHRF1 binds selectively to hemimethylated CpG via its conserved SRA (SET- and RING finger-associated) domain. However, the underlying molecular mechanism is not known. Here, we report a 1.95 A resolution crystal structure of the SRA domain of human UHRF1. Using NMR structure-guided mutagenesis, electrophoretic mobility shift assay, and fluorescence anisotropy analysis, we determined key amino acid residues for methyl-DNA binding that are conserved in the SRA domain. PubMed: 18945682DOI: 10.1074/jbc.C800169200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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