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

. 2014 Dec 24;43(2):1216–1230. doi: 10.1093/nar/gku1329

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

© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 3. — Structural basis of cooperative MDA5 binding to long duplex RNA. (A) The front view: deuterium uptake plots of MDA5 peptides involved in inter-molecular interactions (F374-391, K398-409, F630-642, A745-762, V763-785 and I940-959). The data are plotted as percentage deuterium uptake versus time on the logarithmic scale. Red plots indicate MDA5 apo enzyme and purple plots represent +polyIC state, showing that these surface peptides are more protected against HDX in the presence of polyIC. These peptides are colored in blue and mapped to MDA5 front surface. The HEL2i surface loop N643-674 (in gray), which is truncated in the reported crystal structure, is also modeled according to its HDX profile. (B) The back view: deuterium uptake plots of the peptides involved in inter-molecular interactions (T489-512, F630642, R850-868, Q877-902 and L913-938). (C) A model displays cooperative binding of three neighboring MDA5 monomers to the long dsRNA. This model is constructed based on our HDX data taking the previous cross-linking experiments into consideration (24,27,42). The front and back interface peptides of the central MDA5 monomer (n) are colored in blue and light blue according to (A) and (B). The interfaces of two neighboring MDA5 monomers (n−1 and n+1) are highlighted as well. See also the Supplementary Movie S1 on the cooperative binding of MDA5 to duplex RNA.