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Structural repertoire of immunoglobulin λ light chains
被引:29
作者:
Chailyan, Anna
[1
]
Marcatili, Paolo
[1
]
Cirillo, Davide
[1
]
Tramontano, Anna
[1
,2
]
机构:
[1] Univ Roma La Sapienza, Dept Biochem Sci, I-00185 Rome I, Italy
[2] Univ Roma La Sapienza, Ist Pasteur Fdn Cenci Bolognetti, I-00185 Rome I, Italy
关键词:
immunoglobulins;
canonical structures;
lambda chains;
VARIABLE REGION;
CANONICAL STRUCTURES;
RANDOM FOREST;
ANTIBODY;
KAPPA;
CLASSIFICATION;
CONFORMATION;
HUMANIZATION;
MECHANISM;
SEQUENCES;
D O I:
10.1002/prot.22979
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
The immunoglobulin lambda iso-type 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 kappa and heavy chains. We show here that an analysis of the structures of lambda 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 lambda chains is different and more varied than that of the kappa 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; 79: 1513-1524. (C) 2011 Wiley-Liss, Inc.
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页码:1513 / 1524
页数:12
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