Crystal structure determination of anti‐DNA Fab A52
- 22 January 2014
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 82 (8) , 1674-1678
- https://doi.org/10.1002/prot.24514
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.Keywords
Funding Information
- DOE Office of Biological and Environmental Research, National Institutes of Health
- National Institute of General Medical Sciences (P41GM103393)
- National Center for Research Resources (P41RR001209)
- Israel Science Foundation, United-States Israel Binational Science Foundation
This publication has 41 references indexed in Scilit:
- Towards automated crystallographic structure refinement with phenix.refineActa Crystallographica Section D-Biological Crystallography, 2012
- Crystal structure of an RNA polymerase ribozyme in complex with an antibody fragmentPhilosophical Transactions Of The Royal Society B-Biological Sciences, 2011
- A New Clustering of Antibody CDR Loop ConformationsPublished by Elsevier ,2010
- Synthetic antibodies for specific recognition and crystallization of structured RNAProceedings of the National Academy of Sciences, 2008
- Impact of DNA Hairpin Folding Energetics on Antibody–ssDNA AssociationJournal of Molecular Biology, 2007
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- Electrostatics of nanosystems: Application to microtubules and the ribosomeProceedings of the National Academy of Sciences, 2001
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Structural Families in Loops of Homologous Proteins: Automatic Classification, Modelling and Application to AntibodiesJournal of Molecular Biology, 1996
- Canonical structures for the hypervariable regions of immunoglobulinsJournal of Molecular Biology, 1987