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Biomolecules
Volume 5
Issue 3
10.3390/biom5031955
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Comparative Geometrical Analysis of Leucine-Rich Repeat Structures in the Nod-Like and Toll-Like Receptors in Vertebrate Innate Immunity

by
Norio Matsushima
1,*,
Hiroki Miyashita
1,
Purevjav Enkhbayar
2 and
Robert H. Kretsinger
3
1
The Institute of Tandem Repeats, Sapporo 060-8556, Japan
2
Department of Information and Computer Science, School of Engineering and Applied Sciences, National University of Mongolia, Ulaanbaatar 210646/377, Mongolia
3
Department of Biology, University of Virginia, Charlottesville, VA 22904, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Jürg Bähler
Biomolecules 2015, 5(3), 1955-1978; https://doi.org/10.3390/biom5031955
Received: 21 July 2015 / Revised: 10 August 2015 / Accepted: 11 August 2015 / Published: 18 August 2015
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Abstract

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 β-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 β-strand at the C-terminal side is involved in protein, protein/ligand interactions, but not the descending lateral surface on the opposite side. View Full-Text
Keywords: TLRs; NLRs; receptor; RP105; CD14; helix; dimer TLRs; NLRs; receptor; RP105; CD14; helix; dimer
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MDPI and ACS Style

Matsushima, N.; Miyashita, H.; Enkhbayar, P.; Kretsinger, R.H. Comparative Geometrical Analysis of Leucine-Rich Repeat Structures in the Nod-Like and Toll-Like Receptors in Vertebrate Innate Immunity. Biomolecules 2015, 5, 1955-1978. https://doi.org/10.3390/biom5031955

AMA Style

Matsushima N, Miyashita H, Enkhbayar P, Kretsinger RH. Comparative Geometrical Analysis of Leucine-Rich Repeat Structures in the Nod-Like and Toll-Like Receptors in Vertebrate Innate Immunity. Biomolecules. 2015; 5(3):1955-1978. https://doi.org/10.3390/biom5031955

Chicago/Turabian Style

Matsushima, Norio, Hiroki Miyashita, Purevjav Enkhbayar, and Robert H. Kretsinger. 2015. "Comparative Geometrical Analysis of Leucine-Rich Repeat Structures in the Nod-Like and Toll-Like Receptors in Vertebrate Innate Immunity" Biomolecules 5, no. 3: 1955-1978. https://doi.org/10.3390/biom5031955

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