2011
DOI: 10.1371/journal.pone.0021614
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LRR Conservation Mapping to Predict Functional Sites within Protein Leucine-Rich Repeat Domains

Abstract: Computational prediction of protein functional sites can be a critical first step for analysis of large or complex proteins. Contemporary methods often require several homologous sequences and/or a known protein structure, but these resources are not available for many proteins. Leucine-rich repeats (LRRs) are ligand interaction domains found in numerous proteins across all taxonomic kingdoms, including immune system receptors in plants and animals. We devised Repeat Conservation Mapping (RCM), a computational… Show more

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Cited by 49 publications
(62 citation statements)
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“…Different domains of the NLR were identified based the homology to the annotated RPM1 protein 44 . The most probable LRR motifs were predicted using the LRR conservation mapping tool v2.0 (www.plantpath.wisc.edu/RCM) 45 .…”
Section: Lr22a Protein Domain Predictionmentioning
confidence: 99%
“…Different domains of the NLR were identified based the homology to the annotated RPM1 protein 44 . The most probable LRR motifs were predicted using the LRR conservation mapping tool v2.0 (www.plantpath.wisc.edu/RCM) 45 .…”
Section: Lr22a Protein Domain Predictionmentioning
confidence: 99%
“…The extracellular LRR of EFR is highly glycosylated, which seems to be important for ligand binding as mutation of a single predicted glycosylation site compromises elf18 binding despite correct localization of the mutated protein to the plasma membrane (85). Elf18 most likely binds to the concave surface of the horseshoe-like LRR as mutations of predicted ligand-binding sites identified by several computational methods compromise EFR-mediated immune responses (89).…”
Section: Innate Immunity Mediated By Efrmentioning
confidence: 99%
“…Leucine-rich repeats (LRR) are ligand interaction domains found in various types of proteins. The ubiquity of the domain may be due to its ability to interact with a wide range of substrates (Helft et al 2011). LRR are particularly important for protein-protein interactions (Bella et al 2008) and mechanism of ice-recrystallisation inhibition might be guided by the presence of LRR and IRI patterns in protein sequences (Muthukumaran et al 2011).…”
Section: Discussionmentioning
confidence: 99%