Abstract
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. © 2011 Wiley-Liss, Inc.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1513-1524 |
| Number of pages | 12 |
| Journal | Proteins: Structure, Function, and Bioinformatics |
| Volume | 79 |
| Issue number | 5 |
| DOIs | |
| State | Published - Mar 1 2011 |
| Externally published | Yes |
Bibliographical note
KAUST Repository Item: Exported on 2020-10-01Acknowledged KAUST grant number(s): KUK-I1-012-43
Acknowledgements: Grant sponsor: King Abdullah University of Science and Technology (KAUST); Grant number: KUK-I1-012-43; Grant sponsor: Ministero della Salute; Grant number: RF-IDI-2006-354931; Grant sponsor: FIRB Italbionet and Proteomica
This publication acknowledges KAUST support, but has no KAUST affiliated authors.