Communication pathways bridge local and global conformations in an IgG4 antibody
Abstract The affinity of an antibody for its antigen is primarily determined by the specific sequence and structural arrangement of the complementarity-determining regions (CDRs). Recent evidence, however, points toward a nontrivial relation between the CDR and distal sites: variations in the bindin...
Saved in:
Main Authors: | Thomas Tarenzi, Marta Rigoli, Raffaello Potestio |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2021
|
Subjects: | |
Online Access: | https://doaj.org/article/66ff6bb769b24adb806d3721acdfc7ae |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Nanoscale spatial dependence of avidity in an IgG1 antibody
by: Agnieszka Jendroszek, et al.
Published: (2021) -
Impact of Antigen Density on the Binding Mechanism of IgG Antibodies
by: Maya Hadzhieva, et al.
Published: (2017) -
Cytoprotective IgG antibodies in sera from a subset of patients with AQP4-IgG seropositive neuromyelitis optica spectrum disorder
by: Lukmanee Tradtrantip, et al.
Published: (2021) -
Assignment of Serotype-Specific IgG1, IgG2, and IgA Weight-Based Antibody Units to the Human Pneumococcal Standard Reference Serum, 007sp
by: Scott Jones, et al.
Published: (2019) -
A new approach to produce IgG4-like bispecific antibodies
by: Caizhi Zhao, et al.
Published: (2021)