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Crystal structure determination of anti-DNA Fab A52

Authors

  • Robyn L. Stanfield,

    Corresponding author
    1. The Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California
    • Correspondence to: Robyn L. Stanfield, The Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037. E-mail: robyn@scripps.edu and Dan Eilat, Department of Medicine, Hadassah University Hospital and The Hebrew University Faculty of Medicine, Jerusalem 91120, Israel. E-mail: eilatd@cc.huji.ac.il

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  • Dan Eilat

    1. Department of Medicine, Hadassah University Hospital and The Hebrew University Faculty of Medicine, Jerusalem, Israel
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ABSTRACT

A52 is a murine monoclonal antibody isolated from autoimmune New Zealand Black/New Zealand White F1 mice that recognizes single and double stranded DNA. This mouse strain spontaneously develops systemic lupus erythematosus-like symptoms and has served as a model for that disease for many years. The 1.62 Å crystal structure of the A52 Fab fragment reveals an H3 complementarity determining region with four closely spaced arginine residues, creating a positively charged surface to accommodate bound DNA. Proteins 2014; 82:1674–1678. © 2014 Wiley Periodicals, Inc.

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