Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81819
Title: mAb806 binding to epidermal growth factor receptor: a computational study
Authors: Ng, Yao Zong
Kannan, Srinivasaraghavan
Lane, David P.
Fuentes, Gloria
Verma, Chandra Shekhar
Keywords: EGFR
extracellular domain
Issue Date: 2014
Source: Ng, Y. Z., Kannan, S., Lane, D. P., Fuentes, G., & Verma, C. S. (2015). mAb806 binding to epidermal growth factor receptor: a computational study. Proteins: Structure, Function, and Bioinformatics, 83(1), 153-168.
Series/Report no.: Proteins: Structure, Function, and Bioinformatics
Abstract: The epidermal growth factor receptor (EGFR) is an important target in the treatment of cancer. A very potent antibody, mAb806, has been developed against overexpressed EGFR and was found to be particularly active in brain tumors. Structural studies reveal that it binds to an epitope on the extracellular region of the EGFR. However, this epitope is cryptic/buried in crystal structures of the active (untethered) and inactive (tethered) EGFR, and it is unclear as to how the antibody interacts with this region. To explore this interaction, we combined molecular docking, steered molecular dynamics, and equilibrium molecular dynamics simulations. Our computational models reveal that the antibody induces local unfolding around the epitope to form the antibody–EGFR complex. In addition, regions in the vicinity of the epitope also modulate the interaction, which are in accordance with several other known antibody–antigen interactions, and offers new possibilities for the design of antibodies with increased potency and specificity for this receptor.
URI: https://hdl.handle.net/10356/81819
http://hdl.handle.net/10220/40979
ISSN: 0887-3585
DOI: 10.1002/prot.24714
Schools: School of Biological Sciences 
Rights: © 2014 Wiley Periodicals.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

SCOPUSTM   
Citations 50

3
Updated on Jun 18, 2024

Web of ScienceTM
Citations 50

3
Updated on Oct 26, 2023

Page view(s) 50

528
Updated on Jun 19, 2024

Google ScholarTM

Check

Altmetric


Plumx

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.