PDBsum entry 2lwp

Apoptosis

PDB id: 2lwp

Contents

Protein chain

97 a.a.

PDB id:

2lwp

Name:

Apoptosis

Title:

The nmr solution structure of the the ubiquitin homology domain of mouse bag-1

Structure:

Bag family molecular chaperone regulator 1. Chain: a. Synonym: bag-1, bcl-2-associated athanogene 1. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: bag1. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

18 models

Authors:

H.Huang,C.Yu

Key ref:

H.W.Huang and C.Yu (2013). 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. PubMed id: 23277101

Date:

05-Aug-12 Release date: 19-Jun-13

Protein chain

Q60739  (BAG1_MOUSE) -  BAG family molecular chaperone regulator 1 from Mus musculus

Seq: 355 a.a.

Struc: 97 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Biochem Biophys Res Commun 431:86-91 (2013)

PubMed id: 23277101

The NMR solution structure of the ubiquitin homology domain of Bcl-2-associated athanogene 1 (BAG-1-UBH) from Mus musculus.

H.W.Huang, C.Yu.

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.