Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2019 Mar 14;9:4482. doi: 10.1038/s41598-019-40461-5

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Electrostatic interactions in the IFNγR-A6 complex and the SPR response profiles of the wild-type and the alanine mutant complexes. (a) Crystal structure of the antigen (cyan) and antibody (H chain: green, L chain: magenta) complex (from PDB ID: 1JRH, only variable regions are shown). (b) Electrostatic interactions at the interface of the wild-type complex. Each distance of electrostatic interaction is displayed as dash lines and was measured based on the crystal structure. Antibody variable regions are numbered based on the Kabat numbering scheme. SPR response profiles of (c) Ag:WT-Ab:WT, (d) Ag:K52A-Ab:WT (e) Ag:R84A-Ab:WT, and (f) Ag:K98A-Ab:WT. The concentrations of the antibody were 1000, 500, 250, 125, 62.5, and 31.25 nM. Raw data are in black; red lines are fitted curves. All fitted data were normalized and assume a 1:1 interaction. Binding kinetics were measured at 298 K.