2M5V

Three-dimensional structure of human NLRP10/PYNOD pyrin domain

Summary for 2M5V

• Entry DOI: 10.2210/pdb2m5v/pdb
• NMR Information: BMRB: 18242
• Descriptor: NACHT, LRR and PYD domains-containing protein 10 (1 entity in total)
• Functional Keywords: nlrp10, pynod, pyrin domain, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q86W26
• Total number of polymer chains: 1
• Total formula weight: 11582.62

Authors

Su, M.Y.,Chang, C.F.,Chang, C.I. (deposition date: 2013-03-11, release date: 2013-04-03, Last modification date: 2024-05-15)

Primary citation

Su, M.Y.,Kuo, C.I.,Chang, C.F.,Chang, C.I.
Three-Dimensional Structure of Human NLRP10/PYNOD Pyrin Domain Reveals a Homotypic Interaction Site Distinct from Its Mouse Homologue.
Plos One, 8:e67843-e67843, 2013

PubMed Abstract: NLRPs (Nucleotide-binding domain, leucine-rich repeat and pyrin domain containing proteins) are a family of pattern-recognition receptors (PRRs) that sense intracellular microbial components and endogenous stress signals. NLRP10 (also known as PYNOD) is a unique NLRP member characterized by a lack of the putative ligand-binding leucine-rich repeat domain. Recently, human NLRP10 has been shown to inhibit the self-association of ASC into aggregates and ASC-mediated procaspase-1 processing. However, such activities are not found in mouse NLRP10. Here we report the solution structure and dynamics of human NLRP10 pyrin domain (PYD), whose helix H3 and loop H2-H3 adopt a conformation distinct from those of mouse NLRP10. Docking studies show that human and mouse NLRP10 PYDs may interact differently with ASC PYD. These results provide a possible structural explanation for the contrasting effect of NLRP10 on ASC aggregation in human cells versus mouse models. Finally, we also provide evidence that in human NLRP10 the PYD domain may not interact with the NOD domain to regulate its intrinsic nucleotide hydrolysis activity.

PubMed: 23861819
DOI: 10.1371/journal.pone.0067843

Experimental method

SOLUTION NMR