2LWP
The NMR solution structure of the the ubiquitin homology domain of mouse BAG-1
Summary for 2LWP
| Entry DOI | 10.2210/pdb2lwp/pdb |
| NMR Information | BMRB: 18416 |
| Descriptor | BAG family molecular chaperone regulator 1 (1 entity in total) |
| Functional Keywords | proteasomal degradation, apoptosis |
| Biological source | Mus musculus (mouse) |
| Cellular location | Isoform 1: Nucleus. Isoform 2: Cytoplasm: Q60739 |
| Total number of polymer chains | 1 |
| Total formula weight | 10799.41 |
| Authors | |
| Primary citation | 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 Cited by 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: 23277101DOI: 10.1016/j.bbrc.2012.12.082 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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