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The Allosteric Effect in Antibody-Antigen Recognition

  1. Author:
    Zhao, Jun
    Nussinov,Ruth
    Ma, Buyong

  2. Author Address

    Cancer and Inflammation Program, National Cancer Institute, Frederick, MD, USA., Basic Science Program, Leidos Biomedical Research, Inc. Cancer and Inflammation Program, National Cancer Institute, Frederick, MD, USA., Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel., Basic Science Program, Leidos Biomedical Research, Inc. Cancer and Inflammation Program, National Cancer Institute, Frederick, MD, USA. mabuyong@sjtu.edu.cn.,
    1. Year: 2021
  2. Journal: Methods in molecular biology (Clifton, N.J.)
    1. 2253
    2. Pages: 175-183
  4. Type of Article: Book Chapter
  5. ISSN: 978-1-0716-1153-1
  1. Abstract:

    We studied the molecular details of the recognition of antigens by the variable domain of their cognate antibodies in as well as those elicited by the constant domains, which do not directly interact with antigens. Such effects are difficult to study experimentally; however, molecular dynamics simulations and subsequent residue interaction network analysis provide insight into the allosteric communication between the antigen-binding CDR region and the constant domain. We performed MD simulations of the complex of Fab and prion-associated peptide in the apo and bound forms and follow the conformational changes in the antibody and cross-talk between its subunits and with antigens. These protocols could be generally applied for studies of other antigens-antibody recognition systems.

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External Sources

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  2. DOI: 10.1007/978-1-0716-1154-8_11
  3. PMID: 33315224
  4. View record in Web of Science®
  5. WOS: 000706803800012

Library Notes

  1. Fiscal Year: FY2020-2021
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