2M5V

Three-dimensional structure of human NLRP10/PYNOD pyrin domain

2M5V の概要

• エントリーDOI: 10.2210/pdb2m5v/pdb
• NMR情報: BMRB: 18242
• 分子名称: NACHT, LRR and PYD domains-containing protein 10 (1 entity in total)
• 機能のキーワード: nlrp10, pynod, pyrin domain, immune system
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q86W26
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11582.62

構造登録者

Su, M.Y.,Chang, C.F.,Chang, C.I. (登録日: 2013-03-11, 公開日: 2013-04-03, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

SOLUTION NMR