2LWP

The NMR solution structure of the the ubiquitin homology domain of mouse BAG-1

2LWP の概要

• エントリーDOI: 10.2210/pdb2lwp/pdb
• NMR情報: BMRB: 18416
• 分子名称: BAG family molecular chaperone regulator 1 (1 entity in total)
• 機能のキーワード: proteasomal degradation, apoptosis
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Isoform 1: Nucleus. Isoform 2: Cytoplasm: Q60739
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10799.41

構造登録者

Huang, H.,Yu, C. (登録日: 2012-08-05, 公開日: 2013-06-19, 最終更新日: 2024-05-15)

主引用文献

Huang, H.W.,Yu, C.
The NMR solution structure of the ubiquitin homology domain of Bcl-2-associated athanogene 1 (BAG-1-UBH) from Mus musculus.
Biochem.Biophys.Res.Commun., 431:86-91, 2013

PubMed Abstract: BAG-1 (Bcl-2-associated athanogene 1), a multifunctional anti-apoptotic protein known to interact with various cellular proteins, was isolated using its interaction with the anti-apoptotic protein, Bcl-2. A 97-amino acid segment that includes the ubiquitin homology (UBH) domain of mouse BAG-1 (mBAG-1) interacts with a peptide corresponding to the cytoplasmic tail (CT) domain of proHB-EGF. This protein-peptide interaction is likely to have functional significance, as the two species exhibit a synergistic cytoprotective effect. In this study, we determined the solution structure of mBAG-1-UBH and investigated its interaction with the proHB-EGF-CT peptide using isothermal titration calorimetry and NMR spectroscopy. The solution structure of mBAG-1-UBH was shown to be similar to the previously reported structure of hBAG-1-UBH (PDB code 1WXV). However, their electrostatic potential maps demonstrated some differences in the UBH motifs that may be important for protein-peptide interaction. An NMR titration experiment demonstrated that residues 23-26 and residues 89-94 of mBAG-1-UBH are important for its molecular interaction with the peptide proHB-EGF-CT. BAG-1-UBH shares some biological functions with ubiquitin including the formation of polyubiquitin chain and the proteasomal protein degradation. The unique cytoprotective activity suggests mBAG-1-UBH to be an interesting ubiquitin-like protein with distinct biological functions. Here, we first reported the solution structure of mBAG-1-UBH and the growth factor precursor-interacting motif on the protein. For detail understanding about the binding interface and the mechanism of interaction, the study on mBAG-1-UBH/proHB-EGF-CT complex structure is necessary.

PubMed: 23277101
DOI: 10.1016/j.bbrc.2012.12.082

実験手法

SOLUTION NMR