3UN9

Crystal structure of an immune receptor

Summary for 3UN9

• Entry DOI: 10.2210/pdb3un9/pdb
• Descriptor: NLR family member X1, PLATINUM (II) ION (3 entities in total)
• Functional Keywords: leucine rich repeat (lrr), antiviral signaling, mavs, traf6, ikk, uqcrc2, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion outer membrane: Q86UT6
• Total number of polymer chains: 3
• Total formula weight: 122626.32

Authors

Hong, M.,Yoon, S.I.,Wilson, I.A. (deposition date: 2011-11-15, release date: 2012-03-28, Last modification date: 2024-02-28)

Primary citation

Hong, M.,Yoon, S.I.,Wilson, I.A.
Structure and Functional Characterization of the RNA-Binding Element of the NLRX1 Innate Immune Modulator.
Immunity, 36:337-347, 2012

PubMed Abstract: Mitochondrial NLRX1 is a member of the family of nucleotide-binding domain and leucine-rich-repeat-containing proteins (NLRs) that mediate host innate immunity as intracellular surveillance sensors against common molecular patterns of invading pathogens. NLRX1 functions in antiviral immunity, but the molecular mechanism of its ligand-induced activation is largely unknown. The crystal structure of the C-terminal fragment (residues 629-975) of human NLRX1 (cNLRX1) at 2.65 Å resolution reveals that cNLRX1 consists of an N-terminal helical (LRRNT) domain, central leucine-rich repeat modules (LRRM), and a C-terminal three-helix bundle (LRRCT). cNLRX1 assembles into a compact hexameric architecture that is stabilized by intersubunit and interdomain interactions of LRRNT and LRRCT in the trimer and dimer components of the hexamer, respectively. Furthermore, we find that cNLRX1 interacts directly with RNA and supports a role for NLRX1 in recognition of intracellular viral RNA in antiviral immunity.

PubMed: 22386589
DOI: 10.1016/j.immuni.2011.12.018

Experimental method

X-RAY DIFFRACTION (2.65 Å)