Crystal structure determination of anti‐DNA Fab A52 | Zendy

Stanfield Robyn L. | Zendy; Eilat Dan | Zendy

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Crystal structure determination of anti‐DNA Fab A52

Author(s) -

Stanfield Robyn L.,

Eilat Dan

Publication year - 2014

Publication title -

proteins: structure, function, and bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.699

H-Index - 191

eISSN - 1097-0134

pISSN - 0887-3585

DOI - 10.1002/prot.24514

Subject(s) - dna , chemistry , complementarity (molecular biology) , monoclonal antibody , antibody , microbiology and biotechnology , stereochemistry , biochemistry , biology , immunology , genetics

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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