Biochemical and Biophysical Research Communications
Solution structure of betacellulin, a new member of EGF-family ligands☆
Section snippets
Materials and methods
Sample preparation of BTCe. The expression and purification of recombinant human BTC protein was performed in the same manner as that described in our previous paper [3]. BTCe was obtained as a lysylendo-peptidase product of recombinant human BTC.
For the NMR experiments performed in H2O solution, 3.8 mg of the lyophilized BTCe sample was dissolved in 0.30 ml of H2O (::1) containing 1% acetate buffer to give a final concentration of 2.0 mM (pH 3.5). For the experiments performed in
Chemical shift assignments of BTCe
The chemical shift assignments of BTCe were carried out using the sequential assignment procedure [35] in two-dimensional-NMR experiments performed at 25 °C. The 1H-resonance assignments of all of the main chain atoms, except for the amino proton of the N-terminal Arg31, and most of the side chain atoms of BTCe were unambiguously assigned. The final assignment of 1H-resonances of BTCe at 25 °C has been deposited in the BioMagResBank (Accession Number 4990).
Structural calculation of BTCe
The solution structure of BTCe at 25 °C
Acknowledgements
This work was supported by a grant from the Program for Promotion of Basic Research Activities for Innovative Biosciences (PROBRAIN) to K.K.
References (40)
- et al.
Recombinant human betacellulin. Molecular structure, biological activities, and receptor interaction
J. Biol. Chem.
(1994) - et al.
The structural basis for the specificity of epidermal growth factor and heregulin binding
J. Biol. Chem.
(1995) - et al.
Binding interaction of the heregulinbeta egf domain with ErbB3 and ErbB4 receptors assessed by alanine scanning mutagenesis
J. Biol. Chem.
(1998) - et al.
Structure-function and biological role of betacellulin
Int. J. Biochem. Cell Biol.
(2000) - et al.
Human epidermal growth factor. High resolution solution structure and comparison with human transforming growth factor α
J. Mol. Biol.
(1992) - et al.
Improved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filtering
Biochem. Biophys. Res. Commun.
(1983) - et al.
Coherence transfer by isotropic mixing: application to proton correlation spectroscopy
J. Magn. Reson.
(1983) - et al.
A common sense approach to peak-picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams
J. Magn. Reson.
(1991) - et al.
MOLMOL: a program for display and analysis of macromolecular structures
J. Mol. Graphics
(1996) - et al.
Analogs of human epidermal growth factor which partially inhibit the growth factor-dependent protein-tyrosine kinase activity of the epidermal growth factor receptor
FEBS Lett.
(1990)
Critical functional requirement for the guanidinium group of the arginine 41 side chain of human epidermal growth factor as revealed by mutagenic inactivation and chemical reactivation
J. Biol. Chem.
The significance of valine 33 as a ligand-specific epitope of transforming growth factor α
J. Biol. Chem.
Betacellulin: a mitogen from pancreatic β cell tumors
Science
Betacellulin and activin A coordinately convert amylase-secreting pancreatic AR42J cells into insulin-secreting cells
J. Clin. Invest.
Human betacellulin, a member of the EGF family dominantly expressed in pancreas and small intestine, is fully active in a monomeric form
Growth Factors
Membrane-anchored growth factors
Annu. Rev. Biochem.
Receptor protein-tyrosine kinases and their signal transduction pathways
Annu. Rev. Cell Biol.
Betacellulin activates the epidermal growth factor receptor and erbB-4, and induces cellular response patterns distinct from those stimulated by epidermal growth factor or neuregulin-β
Oncogene
Activation of ErbB4 by the bifunctional epidermal growth factor family hormone epiregulin is regulated by ErbB2
J. Biol. Chem.
The epidermal growth factor receptor couples transforming growth factor-α, heparin-binding epidermal growth factor-like factor, and amphiregulin to Neu, ErbB-3, and ErbB-4
J. Biol. Chem.
Cited by (0)
- ☆
Abbreviations: BTC, betacellulin; BTCe, the EGF-like domain of BTC; CSI, chemical shift index; DQF-COSY, double quantum filtered correlation spectroscopy; DSS, 2,2-dimethyl-2-silapentane-5-sulfonate sodium salt; EGF, epidermal growth factor; EGFR, epidermal growth factor receptor; HRG-α, heregulin-α; HRG-αe, EGF-like domain of heregulin-α; NMR, nuclear magnetic resonance; NOE, nuclear Overhauser effect; NOESY, nuclear Overhauser effect spectroscopy; RMSD, root mean square deviation; SA, simulated annealing; SD, standard deviation; TGF-α, transforming growth factor-α; TOCSY, total correlation spectroscopy. I lost my Debit Card last week, All the particulars like Debit Card No., T-pin No. etc., I have remember my ATM Pin number only. I don't remember my Debit Card No., so I find difficulty to contact by telephone, While I was trying by phone, to communicate
- 1
Current address: Research Institute of Biological Resources, National Institute of Advanced Industrial Science and Technology (AIST), Sapporo 062-8517, Japan.
- 2
Current address: Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.