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Structure-function analysis of a lupus anti-DNA autoantibody: central role of the heavy chain complementarity-determining region 3 Arg in binding of double- and single-stranded DNA

✍ Scribed by Zongdong Li; Edward W. Schettino; Eduardo A. Padlan; Hideyuki Ikematsu; Paolo Casali

Publisher: John Wiley and Sons
Year: 2000
Tongue: English
Weight: 255 KB
Volume: 30
Category: Article
ISSN: 0014-2980
DOI: 10.1002/1521-4141(200007)30:7<2015::aid-immu2015>3.0.co;2-5

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✦ Synopsis

To determine the contribution of the somatic point mutations and that of the complementarity-determining region (CDR)3 Arg to DNA binding, we engineered the germline V H and V ‹ gene revertant and site-mutagenized the CDR3 Arg residues of the mutated and "antigen-selected" mAb 412.67. This anti-DNA autoantibody was derived from B-1 cells of a lupus patient and bore two H-CDR3 Arg, Arg105 and Arg107, encoded by N segment additions, and one ‹ -CDR3 Arg, Arg97, resulting from a point mutation (Kasaian et al. 1994.

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