Proteopedia

2m5v

Three-dimensional structure of human NLRP10/PYNOD pyrin domainThree-dimensional structure of human NLRP10/PYNOD pyrin domain

Structural highlights

2m5v is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NAL10_HUMAN Inhibits autoprocessing of CASP1, CASP1-dependent IL1B secretion, PYCARD aggregation and PYCARD-mediated apoptosis but not apoptosis induced by FAS or BID. Displays anti-inflammatory activity. Plays a role in adaptive immunity through control of dendritic cell-mediated transport of antigen to the lymph nodes from peripheral sites. Required for immunity against C.albicans infection. Involved in the innate immune response by contributing to proinflammatory cytokine release in response to invasive bacterial infection.[1] [2] [3]

Publication Abstract from PubMed

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.

Three-Dimensional Structure of Human NLRP10/PYNOD Pyrin Domain Reveals a Homotypic Interaction Site Distinct from Its Mouse Homologue.,Su MY, Kuo CI, Chang CF, Chang CI PLoS One. 2013 Jul 4;8(7):e67843. doi: 10.1371/journal.pone.0067843. Print 2013. PMID:23861819[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Wang Y, Hasegawa M, Imamura R, Kinoshita T, Kondo C, Konaka K, Suda T. PYNOD, a novel Apaf-1/CED4-like protein is an inhibitor of ASC and caspase-1. Int Immunol. 2004 Jun;16(6):777-86. Epub 2004 Apr 19. PMID:15096476 doi:10.1093/intimm/dxh081
  2. ↑ Imamura R, Wang Y, Kinoshita T, Suzuki M, Noda T, Sagara J, Taniguchi S, Okamoto H, Suda T. Anti-inflammatory activity of PYNOD and its mechanism in humans and mice. J Immunol. 2010 May 15;184(10):5874-84. doi: 10.4049/jimmunol.0900779. Epub 2010 , Apr 14. PMID:20393137 doi:10.4049/jimmunol.0900779
  3. ↑ Lautz K, Damm A, Menning M, Wenger J, Adam AC, Zigrino P, Kremmer E, Kufer TA. NLRP10 enhances Shigella-induced pro-inflammatory responses. Cell Microbiol. 2012 Oct;14(10):1568-83. doi: 10.1111/j.1462-5822.2012.01822.x., Epub 2012 Jun 21. PMID:22672233 doi:10.1111/j.1462-5822.2012.01822.x
  4. ↑ Su MY, Kuo CI, Chang CF, Chang CI. Three-Dimensional Structure of Human NLRP10/PYNOD Pyrin Domain Reveals a Homotypic Interaction Site Distinct from Its Mouse Homologue. PLoS One. 2013 Jul 4;8(7):e67843. doi: 10.1371/journal.pone.0067843. Print 2013. PMID:23861819 doi:10.1371/journal.pone.0067843
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