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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.