Role of antibody heavy and light chain interface residues in affinity maturation of binding to HIV envelope glycoprotein
Author:
Affiliation:
1. The Vanderbilt Vaccine Center
2. Vanderbilt University Medical Center
3. Nashville
4. USA
5. Chemical and Physical Biology Program
6. Department of Chemistry
7. Center for Structural Biology
8. Vanderbilt University
Abstract
Optimization of the heavy chain/light chain interface could serve as an important tool for maximizing antibody/antigen binding affinity without altering antigen contact residues.
Funder
National Institute of Allergy and Infectious Diseases
Publisher
Royal Society of Chemistry (RSC)
Subject
Materials Chemistry,Industrial and Manufacturing Engineering,Process Chemistry and Technology,Energy Engineering and Power Technology,Biomedical Engineering,Chemical Engineering (miscellaneous),Chemistry (miscellaneous)
Link
http://pubs.rsc.org/en/content/articlepdf/2019/ME/C8ME00080H
Reference44 articles.
1. Precise determination of the diversity of a combinatorial antibody library gives insight into the human immunoglobulin repertoire
2. Human Germline Antibody Gene Segments Encode Polyspecific Antibodies
3. The association of heavy and light chain variable domains in antibodies: implications for antigen specificity
4. Analysis and prediction of VH/VL packing in antibodies
5. Related Mechanisms of Antibody Somatic Hypermutation and Class Switch Recombination
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