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2015 ; 5
(3
): 1955-78
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Comparative Geometrical Analysis of Leucine-Rich Repeat Structures in the
Nod-Like and Toll-Like Receptors in Vertebrate Innate Immunity
#MMPMID26295267
Matsushima N
; Miyashita H
; Enkhbayar P
; Kretsinger RH
Biomolecules
2015[Aug]; 5
(3
): 1955-78
PMID26295267
show ga
The NOD-like receptors (NLRs) and Toll-like receptors (TLRs) are pattern
recognition receptors that are involved in the innate, pathogen pattern
recognition system. The TLR and NLR receptors contain leucine-rich repeats (LRRs)
that are responsible for ligand interactions. In LRRs short ?-strands stack
parallel and then the LRRs form a super helical arrangement of repeating
structural units (called a coil of solenoids). The structures of the LRR domains
of NLRC4, NLRP1, and NLRX1 in NLRs and of TLR1-5, TLR6, TLR8, TLR9 in TLRs have
been determined. Here we report nine geometrical parameters that characterize the
LRR domains; these include four helical parameters from HELFIT analysis. These
nine parameters characterize well the LRR structures in NLRs and TLRs; the LRRs
of NLR adopts a right-handed helix. In contrast, the TLR LRRs adopt either a
left-handed helix or are nearly flat; RP105 and CD14 also adopt a left-handed
helix. This geometrical analysis subdivides TLRs into four groups consisting of
TLR3/TLR8/TLR9, TLR1/TLR2/TRR6, TLR4, and TLR5; these correspond to the
phylogenetic tree based on amino acid sequences. In the TLRs an ascending lateral
surface that consists of loops connecting the ?-strand at the C-terminal side is
involved in protein, protein/ligand interactions, but not the descending lateral
surface on the opposite side.