This paper is published as part of a Special issue entitled “Structure and function relationships in proteins: a tribute to Allen B. Edmundson”.
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Review
Structural, antigenic and evolutionary analyses of immunoglobulins and T cell receptors†
Article first published online: 19 NOV 2002
DOI: 10.1002/jmr.586
Copyright © 2002 John Wiley & Sons, Ltd.
Issue
1099-1352/asset/cover.gif?v=1&s=1663ec4b87574b30f56fde6008a20b59ea85eec8 "Journal of Molecular Recognition")
Journal of Molecular Recognition
Special Issue: Structure and Function Relationships in Proteins: A Tribute to Allen B. Edmundson
Volume 15, Issue 5, pages 260–271, September/October 2002
Additional Information
How to Cite
Marchalonis, J. J., Jensen, I. and Schluter, S. F. (2002), Structural, antigenic and evolutionary analyses of immunoglobulins and T cell receptors. J. Mol. Recognit., 15: 260–271. doi: 10.1002/jmr.586
- †
Publication History
- Issue published online: 19 NOV 2002
- Article first published online: 19 NOV 2002
- Manuscript Accepted: 17 JUN 2002
- Manuscript Received: 10 JUN 2002
Funded by
- National Science Foundation. Grant Number: MCB9831846
- Arizona Disease Control Research Commission. Grant Number: 5-038
- Abstract
- Article
- References
- Cited By
Keywords:
- antibodies;
- T cells;
- molecular modeling;
- molecular evolution
Abstract
We have had the pleasure of collaborating with Allen Edmundson for the past 15 years on the structure, binding properties and evolution of immunoglobulins and T cell receptors. Among the most significant contributions of our joint efforts were: (1) the predictive use of structural features of immunoglobulin domains to model the three-dimensional structures of the immunoglobulin domains of human T-cell receptor α and β chains as well as shark light chains and VH domains; (2) the finding that normal humans and other vertebrates express autoantibodies against combining site epitopes of their own T cell receptors; (3) the mapping of the peptide autoepitopes recognized in health, autoimmunity and retroviral infection; and (4) the determination that epitope recognition promiscuity is a characteristic property of the combining sites of IgM immunoglobulins ranging from those of sharks to those of humans. We briefly review the salient findings and status of these studies and indicate the future directions that we will pursue in their continuation. Copyright © 2002 John Wiley & Sons, Ltd.