A 40-kDa epidermal growth factor/transforming growth factor alpha-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor.
作者： D. Kohda , M. Odaka , I. Lax , H. Kawasaki , K. Suzuki
DOI: 10.1016/S0021-9258(18)53950-8
关键词:
摘要: Elucidation of the three-dimensional structure complex epidermal growth factor (EGF) and its receptor is essential for understanding molecular mechanisms EGF-receptor interaction EGF-induced receptor-receptor interaction. NMR useful to investigate interactions in solution between macromolecules at atomic resolution, but has a limitation masses target proteins: less than 300 residues. We have prepared fragment with apparent mass 40 kDa SDS gels from soluble extracellular domain EGF (sEGFR, 619 residues) by sequential limited proteolysis proteinase K bromelain. This monomeric structural consisting 202 amino acid residues (Cys302-Arg503) 18-kDa sugar chains, binds transforming factor-alpha (TGF alpha). 40-kDa dissociation constant about 1 microM human TGF alpha, which similar that parental sEGFR. sEGFR oligomerizes response while does not, suggesting sequences other this required oligomerization. The ligand-binding described report suitable analysis various physico-chemical approaches such as NMR.
elsevier.com
sci-hub.st 参考文章(38)
R. Zidovetzki, Y. Yarden, J. Schlessinger, T.M. Jovin, Microaggregation of hormone-occupied epidermal growth factor receptors on plasma membrane preparations. The EMBO Journal. ,vol. 5, pp. 247- 250 ,(1986) , 10.1002/J.1460-2075.1986.TB04205.X
E.L. Mayes, M.D. Waterfield, Biosynthesis of the epidermal growth factor receptor in A431 cells. The EMBO Journal. ,vol. 3, pp. 531- 537 ,(1984) , 10.1002/J.1460-2075.1984.TB01842.X
K L Carraway, J G Koland, R A Cerione, Visualization of epidermal growth factor (EGF) receptor aggregation in plasma membranes by fluorescence resonance energy transfer. Correlation of receptor activation with aggregation. Journal of Biological Chemistry. ,vol. 264, pp. 8699- 8707 ,(1989) , 10.1016/S0021-9258(18)81849-X
C. Greenfield, I. Hiles, M.D. Waterfield, M. Federwisch, A. Wollmer, T.L. Blundell, N. McDonald, Epidermal growth factor binding induces a conformational change in the external domain of its receptor. The EMBO Journal. ,vol. 8, pp. 4115- 4123 ,(1989) , 10.1002/J.1460-2075.1989.TB08596.X
Larry D. Ward, [22] Measurement of ligand binding to proteins by fluorescence spectroscopy Methods in Enzymology. ,vol. 117, pp. 400- 414 ,(1985) , 10.1016/S0076-6879(85)17024-2
C. Greenfield, G. Patel, S. Clark, N. Jones, M. D. Waterfield, Expression of the human EGF receptor with ligand-stimulatable kinase activity in insect cells using a baculovirus vector. The EMBO Journal. ,vol. 7, pp. 139- 146 ,(1988) , 10.1002/J.1460-2075.1988.TB02793.X
I. Lax, A.K. Mitra, C. Ravera, D.R. Hurwitz, M. Rubinstein, A. Ullrich, R.M. Stroud, J. Schlessinger, Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor. A low resolution projection structure of the ligand-binding domain. Journal of Biological Chemistry. ,vol. 266, pp. 13828- 13833 ,(1991) , 10.1016/S0021-9258(18)92776-6
D.R. Hurwitz, S.L. Emanuel, M.H. Nathan, N. Sarver, A. Ullrich, S. Felder, I. Lax, J. Schlessinger, EGF induces increased ligand binding affinity and dimerization of soluble epidermal growth factor (EGF) receptor extracellular domain. Journal of Biological Chemistry. ,vol. 266, pp. 22035- 22043 ,(1991) , 10.1016/S0021-9258(18)54741-4
I. Lax, F. Bellot, R. Howk, A. Ullrich, D. Givol, J. Schlessinger, Functional analysis of the ligand binding site of EGF-receptor utilizing chimeric chicken/human receptor molecules. The EMBO Journal. ,vol. 8, pp. 421- 427 ,(1989) , 10.1002/J.1460-2075.1989.TB03393.X
K Wüthrich, Protein structure determination in solution by NMR spectroscopy. Journal of Biological Chemistry. ,vol. 265, pp. 22059- 22062 ,(1990) , 10.1016/S0021-9258(18)45665-7