The leucine-rich repeat as a protein recognition motif.

By Bostjan Kobe, A. Kajava. Current Opinion in Structural Biology, 2001

1,685 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/67191c6ff34ea95e4e3f62333df25f9a597567f1

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Citations in the corpus

The Arabidopsis Receptor Kinase FLS2 Binds flg22 and Determines the Specificity of Flagellin Perception[W] (2005, background): “Generally, LRR domains are implicated in protein–protein interactions (Kobe and Kajava, 2001); therefore, we hypothesize that the LRR domain of FLS2 is responsible for interaction with flagellin.”
Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. (2007, neutral): “After many unsuccessful attempts we realized that the ‘‘LxxLxLxxN’’ regions of the LRR modules would be the best fusion sites because they are highly conserved and their structures are practically invariant (Kajava, 1998; Kobe and Kajava, 2001) so that one can predict the structure of the resulting ”
Protein tandem repeats: the more perfect the less structured (2010, background): “…from 5 to 50 residues gained special interest in the 1990s, when several unusual structural folds, including b -helices [3], b -rolls [4], the horseshoe-shaped structure of leucine-rich-repeat proteins [5], b -propellers [6], and a -helical solenoids [7], were resolved by X-ray crystallography.”
The SCF ubiquitin ligase: insights into a molecular machine (2004, background): “uk/interpro/DisplayIproEntry?ac=IPR001611">LRR )), the domain is an arc-shaped α–β-repeat structure that is also found in many protein-binding contexts, including the extracellular-binding domain of certain surface receptor”
NALPs: a novel protein family involved in inflammation (2003, background): “The probable purpose of the LRRs is to provide a versatile structural framework for the formation of protein–protein or protein–carbohydrate/lipid interactions of either pathogenic or cellular origi”
Inflammatory caspases and inflammasomes: master switches of inflammation (2007, background): “The structural units are organized in such a way that all the b strands and the helices are parallel to the same axis, resulting in a nonglobular, horseshoe-shaped molecule with the curved b parallel sheet lining the inner circumference of the horseshoe and the a helices the outer circumference.(65)”
De novo identification of highly diverged protein repeats by probabilistic consistency (2008, background): “In vertebrates, for example, tandemly arranged repeats often serve as a structural framework for the formation of protein–protein interactions (Kobe and Kajava, 2001; Li et al., 2006).”
Transcriptional profiling of canola (Brassica napus L.) responses to the fungal pathogen Sclerotinia sclerotiorum (2007, background): “Leucine-rich repeats (LRRs) are 20–29-residue sequence motifs present in a number of proteins with diverse functions, such as hormone– receptor interactions, enzyme inhibition, cell adhesion and cellular trafficking [40].”
Elicitors, effectors, and R genes: the new paradigm and a lifetime supply of questions. (2007, background): “LRR domains are also found in many other proteins in the biological kingdom, and often control ligand binding or protein-protein interaction (17, 96).”