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 7;12:77. doi: 10.1186/s12964-014-0077-3

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

© Du et al.; licensee BioMed Central Ltd. 2014

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 use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

PMC Copyright notice

Protein:protein docking of IRAK-M-DD tetramers onto IRAK-4-DD tetramers or IRAK-2-DD tetramers. (A) IRAK-M-DD interactions predicted to be important for the contact between IRAK-M and IRAK-4 as obtained by unbiased docking of the IRAK-M tetramer (Yellow) onto the bottom surface of the IRAK-4 tetramer structure (Purple) as is present in the myddosome (3MOP.pdb also F). The residues involved in the interaction are shown with their side chains, of which the residues from IRAK-M are labeled with their respective residue name and number. Two interaction types were involved (type I residues L20, P21, P22, A23, R70, type II residues L16, F18, W74, S75, Q78). This orientation was observed for 63% of the 100 best docked events. (B) IRAK-M-DD interactions predicted to be important for the contact between IRAK-M and IRAK-4 as obtained by unbiased docking of the IRAK-M tetramer (Yellow) on the top surface of IRAK-4 tetramer (Purple). The residues involved in the interaction are shown with their side chains, including R97. This orientation was observed for 37% of the 100 best docked events. (C) Potential sandwich of one IRAK-4-DD tetramer in between 2 IRAK-M-DD tetramers by W74 and R97 mediated interactions. The respective predicted IRAK-4 interactions are shown in detail. (D) Docking of mutant IRAK-M-DD predicts increased IRAK-4 interaction with the IRAK-M R70Q mutant through an extra hydrogen bond formed between Q70 in IRAK-M and R54 in IRAK-4. (E) Part of the composite binding site of the free side of the IRAK-2-DD tetramer in the myddosome is shown with three IRAK-M-DD molecules. The contact residues are shown with their side chain. The residues involved in the interaction from IRAK-M are labeled. Three interaction types were involved. F) A proposed whole myddosome structure with IRAK-M-DD tetramer docked on the free side of the IRAK-2-DD tetramer, based on the myddosome structure, 3MOP.pdb.