Activated NOD1 oligomerizes

Stable Identifier
R-HSA-622310
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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NOD1 is activated by iE-DAP in a LRR domain dependent manner. The LRR domain has a negative influence on NOD1 self-association (Inohara et al. 2000); binding of iE-DAP likely causes 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 this observation, NOD1 and NOD2 are believed to form oligomers of this size (Martinon & Tschopp, 2005).

Literature References
PubMed ID Title Journal Year
10329646 Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB

Inohara, N, Koseki, T, del Peso, L, Hu, Y, Yee, C, Chen, S, Carrio, R, Merino, J, Liu, D, Ni, J, Nunez, G

J Biol Chem 1999
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