Volume 79, Issue 5 pp. 1513-1524
Research Article

Structural repertoire of immunoglobulin λ light chains

Anna Chailyan

Anna Chailyan

Department of Biochemical Sciences, Sapienza University of Rome, P.le A. Moro, 5-00185 Rome (I), Italy

Anna Chailyan and Paolo Marcatili contributed equally to this work.

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Paolo Marcatili

Corresponding Author

Paolo Marcatili

Department of Biochemical Sciences, Sapienza University of Rome, P.le A. Moro, 5-00185 Rome (I), Italy

Anna Chailyan and Paolo Marcatili contributed equally to this work.

Department of Biochemical Sciences, Sapienza University of Rome, P.le A. Moro, 5-00185 Rome (I), Italy===Search for more papers by this author
Davide Cirillo

Davide Cirillo

Department of Biochemical Sciences, Sapienza University of Rome, P.le A. Moro, 5-00185 Rome (I), Italy

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Anna Tramontano

Anna Tramontano

Department of Biochemical Sciences, Sapienza University of Rome, P.le A. Moro, 5-00185 Rome (I), Italy

Istituto Pasteur Fondazione Cenci Bolognetti, Sapienza University of Rome, P.le A. Moro, 5-00185 Rome (I), Italy

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First published: 04 January 2011
Citations: 31

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.

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. Proteins 2011; © 2011 Wiley-Liss, Inc.

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