Anna Chailyan and Paolo Marcatili contributed equally to this work.
Structural repertoire of immunoglobulin λ light chains†
Article first published online: 1 MAR 2011
Copyright © 2011 Wiley-Liss, Inc.
Proteins: Structure, Function, and Bioinformatics
Volume 79, Issue 5, pages 1513–1524, May 2011
How to Cite
Chailyan, A., Marcatili, P., Cirillo, D. and Tramontano, A. (2011), Structural repertoire of immunoglobulin λ light chains. Proteins, 79: 1513–1524. doi: 10.1002/prot.22979
Authors' contribution: AT and PM conceived the work and drafted the manuscript. AC, PM, and DC performed the analysis and contributed to drafting the manuscript.
- Issue published online: 12 APR 2011
- Article first published online: 1 MAR 2011
- Accepted manuscript online: 4 JAN 2011 11:19AM EST
- Manuscript Accepted: 22 DEC 2010
- Manuscript Revised: 3 DEC 2010
- Manuscript Received: 30 AUG 2010
- King Abdullah University of Science and Technology (KAUST). Grant Number: KUK-I1-012-43
- Ministero della Salute. Grant Number: RF-IDI-2006-354931
- FIRB Italbionet and Proteomica
- canonical structures;
- lambda chains
The immunoglobulin λ isotype is present in nearly all vertebrates and plays an important role in the human immune system. Despite its importance, few systematic studies have been performed to analyze the structural conformation of its variable regions, contrary to what is the case for κ and heavy chains. We show here that an analysis of the structures of λ chains allows the definition of a discrete set of recurring conformations (canonical structures) of their hypervariable loops and, most importantly, the identification of sequence constraints that can be used to predict their structure. We also show that the structural repertoire of λ chains is different and more varied than that of the κ chains, consistently with the current view of the involvement of the two major light-chain families in complementary strategies of the immune system to ensure a fine tuning between diversity and stability in antigen recognition. Proteins 2011; © 2011 Wiley-Liss, Inc.