Next Article in Journal / Special Issue
Anti-Drug Antibodies: Emerging Approaches to Predict, Reduce or Reverse Biotherapeutic Immunogenicity
Previous Article in Journal
Special Issue: Monoclonal Antibodies
Previous Article in Special Issue
Evaluation of Continuous Membrane Chromatography Concepts with an Enhanced Process Simulation Approach
Article Menu

Export Article

Open AccessReview
Antibodies 2018, 7(2), 18; https://doi.org/10.3390/antib7020018

IgG Antibody 3D Structures and Dynamics

1
Department of Biomedical Sciences, Mercer University School of Medicine, Savannah, GA 31404, USA
2
Department of Clinical Laboratory, Lianyungang Maternal and Child Health Hospital, Lianyungang 222005, China
3
College of Information Science and Technology, Beijing Normal University, Beijing 100875, China
4
The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Received: 8 February 2018 / Revised: 13 April 2018 / Accepted: 16 April 2018 / Published: 19 April 2018
(This article belongs to the Special Issue Analytical Methodologies for Antibodies)
Full-Text   |   PDF [6155 KB, uploaded 9 August 2018]   |  

Abstract

Antibodies are vital for human health because of their ability to function as nature’s drugs by protecting the body from infection. In recent decades, antibodies have been used as pharmaceutics for targeted therapy in patients with cancer, autoimmune diseases, and cardiovascular diseases. Capturing the dynamic structure of antibodies and characterizing antibody fluctuation is critical for gaining a deeper understanding of their structural characteristics and for improving drug development. Current techniques for studying three-dimensional (3D) structural heterogeneity and variability of proteins have limitations in ascertaining the dynamic structural behavior of antibodies and antibody-antigen complexes. Here, we review current techniques used to study antibody structures with a focus on the recently developed individual-particle electron tomography (IPET) technique. IPET, as a particle-by-particle methodology for 3D structural characterization, has shown advantages in studying structural variety and conformational changes of antibodies, providing direct imaging data for biomolecular engineering to improve development and clinical application of synthetic antibodies. View Full-Text
Keywords: single molecule 3D image; individual-particle 3D image; antibody structure; bispecific antibody; electron tomography; individual-particle electron tomography; IPET; 3D structure of IgG; antibody dynamics; antibody engineering; homodimer antibody; structure of bispecific IgG1 single molecule 3D image; individual-particle 3D image; antibody structure; bispecific antibody; electron tomography; individual-particle electron tomography; IPET; 3D structure of IgG; antibody dynamics; antibody engineering; homodimer antibody; structure of bispecific IgG1
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Jay, J.W.; Bray, B.; Qi, Y.; Igbinigie, E.; Wu, H.; Li, J.; Ren, G. IgG Antibody 3D Structures and Dynamics. Antibodies 2018, 7, 18.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Antibodies EISSN 2073-4468 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top