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PDBsum entry 2lwp
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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H.W.Huang,
C.Yu.
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Ref.
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Biochem Biophys Res Commun, 2013,
431,
86-91.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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1h, 15n and 13 c resonance assignments of ubiquitin h of mouse bag-1
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Authors
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H.Huang,
C.Yu.
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Ref.
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TO BE PUBLISHED ...
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