The pH-dependent structural variation of complementarity-determining region H3 in the crystal structures of the Fv fragment from an anti-dansyl monoclonal antibody
- 1 September 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 291 (1) , 117-134
- https://doi.org/10.1006/jmbi.1999.2931
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 40 references indexed in Scilit:
- Antibody engineeringCurrent Opinion in Structural Biology, 1998
- Crystal Structure of the Complex of the Variable Domain of Antibody D1.3 and Turkey Egg White Lysozyme: A Novel Conformational Change in Antibody CDR-L3 Selects for AntigenJournal of Molecular Biology, 1996
- Bound water molecules and conformational stabilization help mediate an antigen-antibody association.Proceedings of the National Academy of Sciences, 1994
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Small rearrangements in structures of Fv and Fab fragments of antibody D 1.3 on antigen bindingNature, 1990
- Extension of molecular replacement: a new search strategy based on Patterson correlation refinementActa Crystallographica Section A Foundations of Crystallography, 1990
- Conformations of immunoglobulin hypervariable regionsNature, 1989
- Canonical structures for the hypervariable regions of immunoglobulinsJournal of Molecular Biology, 1987
- Three-dimensional structure of a complex of antibody with influenza virus neuraminidaseNature, 1987
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977