Modifications to canonical structure sequence patterns: Analysis for L1 and L3
- 5 March 2002
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 47 (2) , 250-254
- https://doi.org/10.1002/prot.10187
Abstract
The conformation of five of the six hypervariable loops that form the antigen-binding site of antibodies is limited to a small set of structures designated as canonical structures. The canonical structure model has been constituted as a fundamental tool for the modeling of antibodies. The detailed study of tens of crystallographic structures of antibodies has shown the validity of this model in the great majority of cases. The robustness of the forecast capacity of this model depends fundamentally on the precision with which the sequence patterns that characterize each canonical structure form can be defined. Nevertheless, due to the enormous quantity of structural information about antibodies generated during the last decade, it is difficult to avoid mistakes or confusion in the model. In the present work, we propose some corrections to the model for loops L1 and L3 that permit defining sequence patterns that avoid confusion and make better forecasting of the canonical structure model possible.Keywords
Funding Information
- Proyectos Estratégicos de la U.V. (1999-2000)
- SNI-CONACyT (to EVM)
This publication has 14 references indexed in Scilit:
- Canonical structures for the hypervariable regions of T cell αβ receptorsJournal of Molecular Biology, 2000
- Standard conformations for the canonical structures of immunoglobulins 1 1Edited by I. A. WilsonJournal of Molecular Biology, 1997
- Sequence and Evolution of the Human Germline VλRepertoireJournal of Molecular Biology, 1996
- Structural Families in Loops of Homologous Proteins: Automatic Classification, Modelling and Application to AntibodiesJournal of Molecular Biology, 1996
- Conformation of the hypervariable region L3 without the key proline residueProtein Science, 1996
- Canonical Structure Repertoire of the Antigen-binding Site of Immunoglobulins Suggests Strong Geometrical Restrictions Associated to the Mechanism of Immune RecognitionJournal of Molecular Biology, 1995
- Crystal Structure of a Catalytic Antibody with a Serine Protease Active SiteScience, 1994
- Conformation of Complementarity Determining Region L1 Loop in Murine IgG λ Light Chain Extends the Repertoire of Canonical FormsJournal of Molecular Biology, 1993
- Framework residue 71 is a major determinant of the position and conformation of the second hypervariable region in the VH domains of immunoglobulinsJournal of Molecular Biology, 1990
- Canonical structures for the hypervariable regions of immunoglobulinsJournal of Molecular Biology, 1987