MDP:NOD2 MDP:NOD2 oligomer Activated NOD2 oligomerizes Authored: Jupe, S, 2010-04-22 Edited: Jupe, S, 2011-04-28 NOD2 is activated by MDP in a LRR domain dependent manner. Based on studies of NOD1 activation and structural data from the NLR-related scaffold Apaf-1, the LRR domain is believed to have a negative influence on NOD2 self-association (Inohara et al. 2000, Riedl & Salvesen 2007); binding of MDP is believed to cause conformational changes that free the NACHT domain, allowing oligomerization and subsequent association of other proteins. Coimmunoprecipitation experiments demonstrate that NOD1 can interact with itself (Inohara et al. 1999) via the NACHT domain (Inohara et al. 2000). NACHT domains are part of the AAA+ domain family. Members of this family form hexamers or heptamers. Based on these observations, NOD2 is generally believed to form hexamers or heptamers (Martinon & Tschopp, 2005). NOD2 oliogomerization has been observed in NOD2-transfected HEK293T cells (Zhao et al. 2007). Pubmed10880512 Pubmed15967716 Pubmed17303577 Pubmed17377525 Reactome Database ID Release 43708349 Reactome, http://www.reactome.org ReactomeREACT_75789 Reviewed: Kufer, TA, 2011-04-28 Reviewed: Rittinger, K, 2011-06-06 Reviewed: Wong, Edmond, 2011-06-06 has a Stoichiometric coefficient of 6