Solution Structure of the Internal UBA Domain of HHR23A
Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions.
Biochemical and Structural Analysis of the Interaction between the Uba(2) Domain of the DNA Repair Protein Hhr23A and HIV-1 Vpr
UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A
1DV0 IS THE C-terminal UBA domain of HHR23A
1F4I IS THE P333E mutant of C-terminal UBA domain of HHR23A
The structure was determined using triple-resonance NMR spectroscopy
50mM sodium phosphate, 100mM sodium chloride
The structures are based on 1692 NOE-derived distance restraints, of which 1055 distance restraints are non-redundant. 407 restraints are intraresidue, 212 are sequential, 226 are mediumrange (i-j < 5) and 210 are long-range (i-j > 4)
50mM phosphate buffer, 100mM sodium chloride 95% H2O, 5% D2O
Ubiquitin associated domain, UBA domain, Ubiquitin proteosome pathway, DNA BINDING PROTEIN
MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTK AGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTG SEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQ FQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQE KEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE