Antibody Elbow Angles are Influenced by their Light Chain Class
Top Cited Papers
- 1 April 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 357 (5) , 1566-1574
- https://doi.org/10.1016/j.jmb.2006.01.023
Abstract
No abstract availableKeywords
Funding Information
- University of California
- Lawrence Livermore National Laboratory (W-7405-Eng-48)
- National Institutes of Health (GM-38273, GM-46192)
- U.S. Department of Energy
This publication has 17 references indexed in Scilit:
- Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein–nucleic acid complex crystalsProtein Science, 2003
- Elbow Flexibility and Ligand-Induced Domain Rearrangements in Antibody Fab NC6.8: Large Effects of a Small HaptenBiophysical Journal, 2000
- The Protein Data BankNucleic Acids Research, 2000
- Antibody-antigen interactions: new structures and new conformational changesCurrent Opinion in Structural Biology, 1994
- How the anti-(metal chelate) antibody CHA255 is specific for the metal ion of its antigen: X-ray structures for two Fab'/hapten complexes with different metals in the chelateBiochemistry, 1993
- Elbow motion in the immunoglobulins involves a molecular ball-and-socket jointNature, 1988
- Phosphocholine binding immunoglobulin Fab McPC603Journal of Molecular Biology, 1986
- Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolutionJournal of Molecular Biology, 1980
- Crystallographic structure studies of an IgG molecule and an Fc fragmentNature, 1976
- Structure of a λ-type Bence-Jones protein at 3.5-Å resolutionBiochemistry, 1973