3DWH: Structural And Functional Analysis Of Sra Domain

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.
PDB ID: 3DWHDownload
MMDB ID: 67484
PDB Deposition Date: 2008/7/22
Updated in MMDB: 2008/10
Experimental Method:
x-ray diffraction
Resolution: 1.95  Å
Source Organism:
Similar Structures:
Biological Unit for 3DWH: monomeric; determined by author and by software (PISA)
Molecular Components in 3DWH
Label Count Molecule
Protein (1 molecule)
E3 Ubiquitin-protein Ligase Uhrf1(Gene symbol: UHRF1)
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB