Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (10)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by McInnes, C.
Right arrow Articles by Sykes, B. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McInnes, C.
Right arrow Articles by Sykes, B. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 13, No. 3, 143-147, March 2000
© 2000 Oxford University Press

NMR study of the differential contributions of residues of transforming growth factor alpha to association with its receptor

Campbell McInnes1, Suzanne Grothe2, Maureen O'Connor-McCourt2 and Brian D. Sykes1,3

1 Protein Engineering Network of Centres of Excellence, 713 Heritage Medical Research Centre, University of Alberta, Edmonton, Alberta, T6G 2S2 and 2 Biotechnology Research Institute, Montreal, Quebec, H4P 2R2, Canada

A heteronuclear NMR study of human transforming growth factor alpha (TGF{alpha}) in complex with the epidermal growth factor receptor extracellular domain (EGFR-ED) provided an effective method for delineating the relative contributions of the residues of the ligand to its affinity for the receptor. In conjunction with previously obtained mutagenesis data, these results indicate that while a large number of residues are involved in complex formation and make up the binding interface, a small subset contribute most of the binding energy. They also show that while the residues which contribute to receptor binding are localized on one face of the molecule, the specific residues that play the major role in the affinity of TGF{alpha} in the complex are in two distinct regions of TGF{alpha}. This suggests that two small functional epitopes each composed of two residues exist within a larger structural epitope presented on the binding face. These results give the most detailed picture to date of the receptor binding determinants and yield further insight into the formation of the ligand–receptor complex.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
T. Aizawa, Y. Hayakawa, A. Ohnishi, N. Fujitani, K. D. Clark, M. R. Strand, K. Miura, N. Koganesawa, Y. Kumaki, M. Demura, et al.
Structure and Activity of the Insect Cytokine Growth-blocking Peptide. ESSENTIAL REGIONS FOR MITOGENIC AND HEMOCYTE-STIMULATING ACTIVITIES ARE SEPARATE
J. Biol. Chem., August 17, 2001; 276(34): 31813 - 31818.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.