Skip Navigation


PEDS Advance Access originally published online on June 13, 2006
Protein Engineering Design and Selection 2006 19(8):377-384; doi:10.1093/protein/gzl022
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
19/8/377    most recent
gzl022v1
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 (4)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Epa, V.C.
Right arrow Articles by Ward, C. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Epa, V.C.
Right arrow Articles by Ward, C. W.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Model for the complex between the insulin-like growth factor I and its receptor: towards designing antagonists for the IGF-1 receptor

V.Chandana Epa1 and Colin W. Ward

CSIRO Molecular & Health Technologies 343 Royal Parade, Parkville, Victoria 3052, Australia

1To whom correspondence should be addressed. E-mail: Vidana.Epa{at}csiro.au

The type-1 insulin-like growth factor receptor (IGF-1R) is the cognate tyrosine kinase receptor for the insulin-like growth factor IGF-I and is expressed widely in many foetal and postnatal tissue cells. IGF-1R is overexpressed in a number of human tumour types and is a valid target for anti-cancer therapeutic efforts. Designing antagonists for IGF-1R would be greatly facilitated by the availability of structural information on the complex between IGF-I and IGF-1R. In the present work we model the three-dimensional structure of the complex between IGF-I and the first three domains of IGF-1R using a macromolecular docking method guided by selected experimental data. Interface metrics indicative of the binding affinity and reliability of the model are computed and compared with other biomolecular complexes. This model is consistent with experimental chimerical and mutagenesis data, provides a structural basis for understanding the primary interaction of IGF-I with its receptor and facilitates design of antagonist ligands.

Keywords: antagonist design/complementarity/IGF-1R/protein docking

Received December 16, 2005; revised April 5, 2006; accepted May 14, 2006.


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
L. Gauguin, C. Delaine, C. L. Alvino, K. A. McNeil, J. C. Wallace, B. E. Forbes, and P. De Meyts
Alanine Scanning of a Putative Receptor Binding Surface of Insulin-like Growth Factor-I
J. Biol. Chem., July 25, 2008; 283(30): 20821 - 20829.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Endocrinol. Metab.Home page
K. Inagaki, A. Tiulpakov, P. Rubtsov, P. Sverdlova, V. Peterkova, S. Yakar, S. Terekhov, and D. LeRoith
A Familial Insulin-Like Growth Factor-I Receptor Mutant Leads to Short Stature: Clinical and Biochemical Characterization
J. Clin. Endocrinol. Metab., April 1, 2007; 92(4): 1542 - 1548.
[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.