Crystal structure of an LRR protein with two solenoids

Liu, Peiyuan; Hu, Zhongzhi; Zhou, Bin; Liu, Simiao; Chai, Jijie

doi:10.1038/cr.2012.159

Cited by 15 publications

(17 citation statements)

References 14 publications

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“…In SG_IX, the crystal structure of the Arabidopsis TRANSMEMBRANE KINASE 1 [TMK1, also known as BLK1 (BARK1-like Kinase 1)] suggests that the islands could be critical for structural integrity. In SG_XV, the crystal structure of RECEPTOR-LIKE PROTEIN KINASE 2 (RPK2, also known as TOAD2) suggests that the islands could be the site for ligand binding as in BRI1 (Liu et al, 2013; Song et al, 2014). …”

Section: Resultsmentioning

confidence: 99%

New Insights on Leucine-Rich Repeats Receptor-Like Kinase Orthologous Relationships in Angiosperms

et al. 2017

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Leucine-Rich Repeats Receptor-Like Kinase (LRR-RLK) genes represent a large and complex gene family in plants, mainly involved in development and stress responses. These receptors are composed of an LRR-containing extracellular domain (ECD), a transmembrane domain (TM) and an intracellular kinase domain (KD). To provide new perspectives on functional analyses of these genes in model and non-model plant species, we performed a phylogenetic analysis on 8,360 LRR-RLK receptors in 31 angiosperm genomes (8 monocots and 23 dicots). We identified 101 orthologous groups (OGs) of genes being conserved among almost all monocot and dicot species analyzed. We observed that more than 10% of these OGs are absent in the Brassicaceae species studied. We show that the ECD structural features are not always conserved among orthologs, suggesting that functions may have diverged in some OG sets. Moreover, we looked at targets of positive selection footprints in 12 pairs of OGs and noticed that depending on the subgroups, positive selection occurred more frequently either in the ECDs or in the KDs.

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Section: Resultsmentioning

confidence: 99%

New Insights on Leucine-Rich Repeats Receptor-Like Kinase Orthologous Relationships in Angiosperms

et al. 2017

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“…The LRR domain of TMK1 features a non-LRR domain, which disrupts the regular repeat structure, creating a sharp kink in the overall assembly (75) (Figure 5d). Although TMK1 has been implicated in the recognition of the auxin-loaded ABP1 protein (auxin being a tryptophanderived plant growth hormone), it is unclear whether the unusual ectodomain structure of TMK1 represents a specific adaptation for the recognition of a large protein ligand (19,137).…”

Section: C)mentioning

confidence: 99%

The Structural Basis of Ligand Perception and Signal Activation by Receptor Kinases

Hohmann

Lau

Hothorn

2017

Annu. Rev. Plant Biol.

219

254

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Plants have evolved a family of unique membrane receptor kinases to orchestrate the growth and development of their cells, tissues, and organs. Receptor kinases also form the first line of defense of the plant immune system and allow plants to engage in symbiotic interactions. Here, we discuss recent advances in understanding, at the molecular level, how receptor kinases with lysin-motif or leucine-rich-repeat ectodomains have evolved to sense a broad spectrum of ligands. We summarize and compare the established receptor activation mechanisms for plant receptor kinases and dissect how ligand binding at the cell surface leads to activation of cytoplasmic signaling cascades. Our review highlights that one family of plant membrane receptors has diversified structurally to fulfill very different signaling tasks.

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“…Five hundred thirty‐seven VS parts from 43 proteins were identified (Table ). Lgr4 and VLR that are “Typical” LRR proteins contain only one Leptospira‐like LRR motif . The one Leptospira‐like LRR was analyzed.…”

Section: Methodsmentioning

confidence: 99%

A strong correlation between consensus sequences and unique super secondary structures in leucine rich repeats

et al. 2020

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Leucine rich repeats (LRRs) are present in over 430 000 proteins from viruses to eukaryotes. The LRRs are 20 to 30 residues long and occur in tandem. Individual LRRs are separated into a highly conserved segment with the consensus of LxxLxLxxNxL or LxxLxLxxNxxL (HCS) and a variable segment (VS). In LRRs parallel stacking of short β‐strands (at positions 3‐5 in HCS) form a super helix arrangement called a solenoid structure. Many classes have been recognized. All three classes of Plant specific, Leptospira‐like, and SDS22‐like LRRs which are 24, 23, and 22 residues long, respectively, form a 3(10)‐helix in the VS part. To get a deeper understanding of sequence, structure correlations in LRR structures, we utilized secondary structure assignment and HELFIT analysis (calculating helix axis, pitch, radius, residues per turn, and handedness) based on the atomic coordinates in crystal structures of 43 LRR proteins. We also defined three structural parameters using the three unit vectors of the helix axes of 3(10)‐helix, β‐turn, and LRR‐domain calculated by HELFIT. The combination of the secondary structure assignment and HELFIT reveals that their LRRs adopt unique super secondary structures consisting of a 3(10)‐helix and one or two Type I β‐turns. We propose one structural parameter as a geometrical invariant of LRR solenoid structures. The common LxxLxxL sequence (where “L” is Leu, Ile, Val, Phe or Cys) in the three classes is an essential determinant for the super secondary structures providing a medium range interaction.

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Crystal structure of an LRR protein with two solenoids

Cited by 15 publications

References 14 publications

New Insights on Leucine-Rich Repeats Receptor-Like Kinase Orthologous Relationships in Angiosperms

New Insights on Leucine-Rich Repeats Receptor-Like Kinase Orthologous Relationships in Angiosperms

The Structural Basis of Ligand Perception and Signal Activation by Receptor Kinases

A strong correlation between consensus sequences and unique super secondary structures in leucine rich repeats

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