title: Structural repertoire of immunoglobulin λ light chains.
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.
authors.affiliation: Department of Biochemical Sciences, Sapienza University of Rome, P.le A. Moro, 5-00185 Rome (I), Italy.
authors.forename: Anna
authors.initials: A
authors.lastname: Chailyan
authors.forename: Paolo
authors.initials: P
authors.lastname: Marcatili
authors.forename: Davide
authors.initials: D
authors.lastname: Cirillo
authors.forename: Anna
authors.initials: A
authors.lastname: Tramontano
mesh_terms: D000818:Animals; D006801:Humans; D007135:Immunoglobulin Variable Region / Q000737:chemistry*; D007146:Immunoglobulin lambda-Chains / Q000737:chemistry*; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D007135:Immunoglobulin Variable Region; D007146:Immunoglobulin lambda-Chains