One leucine-rich repeat variant domain (LRV) has a novel repetitive structural motif consisting of alternating alpha- and 3 10-helices arranged in a right-handed superhelix, with the absence of the beta-sheets present in other leucine-rich repeats.

LRRs (leucine rich repeats) are present in over 14,000 proteins. Non-LRR, island regions (IRs) interrupting LRRs are widely distributed. The present article reviews 19 families of LRR proteins having non-LRR IRs (LRR@IR proteins) from various plant species.

Leucine-rich repeats (LRRs) are 20-29-residue sequence motifs present in a number of proteins with diverse functions. The primary function of these motifs appears to be to provide a versatile structural framework for the formation of protein-protein interactions.

In mammals, toll-like receptors (TLRs) and NOD-like receptors (NLRs) through their LRR domain, sense molecular determinants from a structurally diverse set of bacterial, fungal, parasite and viral-derived components. In humans, at least 34 LRR proteins are implicated in diseases.

Mar 8, 2020 · To address these challenges, in this paper we propose a new LRR motif detection method: LRRpredictor, designed to be more sensitive to motif irregularities than the existing methods like LRRfinder or LRRsearch and to detect irregular and short LRR signatures as are often found in plant NLRs, but not limited to this class.

All TLR ECDs are constructed of tandem copies of a motif known as the leucine-rich repeat (LRR), which is typically 22–29 residues in length and contains hydrophobic residues spaced at distinctive intervals (Figure 1A).

Jan 28, 2021 · The LRR motif signatures in plant LRR-RLKs SG_vii, SG_x, SG_xi and SG_xii with more than 20 LRR repeats. a The consensus sequences of the LRR motif. b The model of a plant LRR unit.

Jan 1, 2025 · LRR-LIKE1 is proposed to mediate jasmonate-dependent abiotic stress signaling by interacting with proteins to regulate reactive oxygen species (ROS) responses and light signaling. Further studies are needed to clarify these mechanisms and their broader implications.

Dec 1, 2001 · Leucine-rich repeats (LRRs) are 20–29-residue sequence motifs present in a number of proteins with diverse functions. The primary function of these motifs appears to be to provide a versatile structural framework for the formation of protein–protein interactions.

Nov 5, 2024 · Leucine-rich repeat (LRR) domains are a type of curved solenoid domain with repeated units of about 20—30 residues long which contain leucine residues in a beta-strand conformation.