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

. 2018 May 31;8:8449. doi: 10.1038/s41598-018-26800-y

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

© The Author(s) 2018

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

Interactions between scFv513 and DIII from DENV4 derived from crystallography. (A) Overall views at two angles separated by 90° of the complex between scFv513 (VH and VL depicted as green and yellow ribbons respectively) and the domain III of the envelope protein from DENV4 (red ribbons). Coordinates were taken from molecule A of PDB code 5AAM. CDRs and N-and C-termini are labeled. (B) Details of the interactions and comparison with 4E11: panels (C) and (D) show a key contact region where an additional salt bridge was introduced in scFv513 between Glu55^H2, (Kabat numbering) and Lys323 (EDIII), which is absent in the complex between scFvE11 and EDIII (panel D). This results from the Ala to Glu substitution in the H2 region of 4E11 (see text). The S26Δ deletion introduced in VH of 513 (white tube) removing the bulge present in 4E11 (blue tube) is displayed in (B) and the movement between the two polypeptide chains is shown by an arrow. The electron density map (coefficients 2Fo-Fc at a level of 1σ) is overlaid in panels (B) and (C).