Structural repertoire of immunoglobulin λ light chains†
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.
Search for more papers by this authorCorresponding 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 authorDavide Cirillo
Department of Biochemical Sciences, Sapienza University of Rome, P.le A. Moro, 5-00185 Rome (I), Italy
Search for more papers by this authorAnna 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
Search for more papers by this authorAnna 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.
Search for more papers by this authorCorresponding 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 authorDavide Cirillo
Department of Biochemical Sciences, Sapienza University of Rome, P.le A. Moro, 5-00185 Rome (I), Italy
Search for more papers by this authorAnna 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
Search for more papers by this authorAuthors' 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.
Supporting Information
Additional Supporting Information may be found in the online version of this article.
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PROT_22979_sm_suppinfotable2.pdf27.9 KB | Supporting Information Table 2 |
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PROT_22979_sm_suppinfotable4.pdf27.9 KB | Supporting Information Table 4 |
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