1IFY

Solution Structure of the Internal UBA Domain of HHR23A

1IFY の概要

• エントリーDOI: 10.2210/pdb1ify/pdb
• 関連するPDBエントリー: 1DV0 1F4I
• 分子名称: UV EXCISION REPAIR PROTEIN RAD23 HOMOLOG A (1 entity in total)
• 機能のキーワード: ubiquitin associated domain, uba domain, ubiquitin proteosome pathway, dna binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P54725
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5496.23

構造登録者

Mueller, T.D.,Feigon, J. (登録日: 2001-04-13, 公開日: 2002-07-03, 最終更新日: 2024-05-22)

主引用文献

Mueller, T.D.,Feigon, J.
Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions.
J.Mol.Biol., 319:1243-1255, 2002

PubMed Abstract: UBA domains are a commonly occurring sequence motif of approximately 45 amino acid residues that are found in diverse proteins involved in the ubiquitin/proteasome pathway, DNA excision-repair, and cell signaling via protein kinases. The human homologue of yeast Rad23A (HHR23A) is one example of a nucleotide excision-repair protein that contains both an internal and a C-terminal UBA domain. The solution structure of HHR23A UBA(2) showed that the domain forms a compact three-helix bundle. We report the structure of the internal UBA(1) domain of HHR23A. Comparison of the structures of UBA(1) and UBA(2) reveals that both form very similar folds and have a conserved large hydrophobic surface patch. The structural similarity between UBA(1) and UBA(2), in spite of their low level of sequence conservation, leads us to conclude that the structural variability of UBA domains in general is likely to be rather small. On the basis of the structural similarities as well as analysis of sequence conservation, we predict that this hydrophobic surface patch is a common protein-interacting surface present in diverse UBA domains. Furthermore, accumulating evidence that ubiquitin binds to UBA domains leads us to the prediction that the hydrophobic surface patch of UBA domains interacts with the hydrophobic surface on the five-stranded beta-sheet of ubiquitin. Detailed comparison of the structures of the two UBA domains, combined with previous mutagenesis studies, indicates that the binding site of HIV-1 Vpr on UBA(2) does not completely overlap the ubiquitin binding site.

PubMed: 12079361
DOI: 10.1016/S0022-2836(02)00302-9

実験手法

SOLUTION NMR