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Journal ArticleDOI

The leucine-rich repeat as a protein recognition motif

TLDR
New structural information has increased the understanding of the structural determinants of LRR proteins and the ability to model such proteins with unknown structures, and has shed new light on how these proteins participate in protein-protein interactions.
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This article is published in Current Opinion in Structural Biology.The article was published on 2001-12-01. It has received 1604 citations till now. The article focuses on the topics: Subfamily & Protein structure.

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A Renaissance of Elicitors: Perception of Microbe-Associated Molecular Patterns and Danger Signals by Pattern-Recognition Receptors

TL;DR: Current evidence indicates that MAMPs, DAMPs, and effectors are all perceived as danger signals and induce a stereotypic defense response, and the importance of MAMP/PRR signaling for plant immunity is highlighted.
Journal ArticleDOI

Mechanism of auxin perception by the TIR1 ubiquitin ligase

TL;DR: These structures show that the leucine-rich repeat domain of TIR1 contains an unexpected inositol hexakisphosphate co-factor and recognizes auxin and the Aux/IAA polypeptide substrate through a single surface pocket, establishing the first structural model of a plant hormone receptor.
Journal ArticleDOI

Crystal Structure of the TLR1-TLR2 Heterodimer Induced by Binding of a Tri-Acylated Lipopeptide

TL;DR: It is proposed that formation of the TLR1-TLR2 heterodimer brings the intracellular TIR domains close to each other to promote dimerization and initiate signaling.
Journal ArticleDOI

Innate immune pattern recognition: a cell biological perspective.

TL;DR: This review highlights aspects of cell biology in pattern-recognition receptor signaling by focusing on signals that originate from the cell surface, from endosomal compartments, and from within the cytosol.
References
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Journal ArticleDOI

The leucine-rich repeat: a versatile binding motif.

TL;DR: The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to beta-alpha structural units, which are arranged so that they form a parallel beta-sheet with one surface exposed to solvent, so that the protein acquires an unusual, nonglobular shape.
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Nod1, an Apaf-1-like Activator of Caspase-9 and Nuclear Factor-κB

TL;DR: Nod1 is a leucine-rich repeat-containing Apaf-1-like molecule that can regulate both apoptosis and NF-κB activation pathways.
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Localization of apical epithelial determinants by the basolateral PDZ protein Scribble.

TL;DR: The results show that the lateral domain of epithelia, particularly the septate junction, functions in restricting apical membrane identity and correctly placing adherens junctions.
Journal ArticleDOI

A structural basis of the interactions between leucine-rich repeats and protein ligands.

TL;DR: The unusual non-globular structure of ribonuclease inhibitor, its solvent-exposed parallel β-sheet and the conformational flexibility of the structure are used in the interaction; they appear to be the principal reasons for the effectiveness of leucine-rich repeats as protein-binding motifs.
Journal ArticleDOI

Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats

TL;DR: This work has determined the crystal structure of the porcine inhibitor, which is the first three-dimensional structure of a protein containing leucine-rich repeats and represents a new class of α/β protein fold.
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