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The NMR solution structure of the ubiquitin homology domain of Bcl-2-associated athanogene 1 (BAG-1-UBH) from Mus musculus.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2013 Feb 01; Vol. 431 (1), pp. 86-91. Date of Electronic Publication: 2012 Dec 28. - Publication Year :
- 2013
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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.<br /> (Copyright © 2013 Elsevier Inc. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Animals
Heparin-binding EGF-like Growth Factor
Humans
Intercellular Signaling Peptides and Proteins chemistry
Mice
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Protein Interaction Mapping
Protein Structure, Tertiary
Solutions
DNA-Binding Proteins chemistry
Transcription Factors chemistry
Ubiquitin chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 431
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 23277101
- Full Text :
- https://doi.org/10.1016/j.bbrc.2012.12.082