Protein Interactions

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Obtained from STRING [1]: NACHT, LRR and PYD-containing protein 1 (Death effector filament- forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain) (Caspase recruitment domain protein 7); Able to form cytoplasmic structures termed death effector filaments. Enhances APAF1 and cytochrome c-dependent activation of pro-caspase-9 and consecutive apoptosis. Stimulates apoptosis through activation of caspase-3. Involved in activation of caspase-1 and caspase-5 as part of the NALP1 inflammasome complex which leads to processing and release of IL1B and IL18. Binds ATP (1477 aa)

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Protein Interaction Map for NLRP1
NLRP1 is a protein associated with an immune response signaling cell death. In subjects without vitiligo, the NLRP1 protein is only activated in the presence of a microbial or viral antigen that stimulates a conformational change in the NLRP1 protein via its PYD, NACHT, and LRR domains. Initially, a viral or bacterial antigen (most commonly muracyl dipeptide (MDP)) is recognized and bound by the LRR domain on the NLRP1 protein. This causes the NACHT domain to oligomerize to the NACHT domain of another NLRP1 protein. Following this oligomerization, a caspase cascade event occurs, in which the CARD domains of the caspases (1 and 5) recognize the CARD domains of the PYD-binding protein and CARD domain of the NLRP1 protein, respectively. Activation of caspases signals an increase in interleukins (abbreviated IL in the map). High levels of interleukins are associated with cell death. As observed in the diagram above, NLRP1 is linked to both  caspases and interleukins. Proteins such as APAF1 and MEFV serve as accessory proteins that aid in efficiency and kinetics of these pathways. In patients with vitiligo, mutations within the NLRP1 gene results in an overactive protein that signals a cell death response constitutively. 

References

[1] STRING: http://string-db.org/newstring_cgi/show_network_section.pl



This Web site was created as project for Genetics 677 at UW-Madison, Spring 2010. 


Sarah Hamilton. May 17, 2010.