Structural principles of leucine‐rich repeat (LRR) proteins

@article{Enkhbayar2004StructuralPO,
  title={Structural principles of leucine‐rich repeat (LRR) proteins},
  author={Purevjav Enkhbayar and Masakatsu Kamiya and Mitsuru Osaki and Takeshi Matsumoto and Norio Matsushima},
  journal={Proteins: Structure},
  year={2004},
  volume={54}
}
LRR‐containing proteins are present in over 2000 proteins from viruses to eukaryotes. Most LRRs are 20–30 amino acids long, and the repeat number ranges from 2 to 42. The known structures of 14 LRR proteins, each containing 4–17 repeats, have revealed that the LRR domains fold into a horseshoe (or arc) shape with a parallel β‐sheet on the concave face and with various secondary structures, including α‐helix, 310‐helix, and pII helix on the convex face. We developed simple methods to charactere… 
Helical Parameters and Correlations of Tandem Leucine Rich Repeats in
TLDR
The program HELFIT is used to assign helical parameters to 642 LRRs of known structures of 114 proteins, and these parameters and their correlations with eight classes of LRR, with the number of repeat units in the L RR, with oligomerization, and with ligand state of the LRR.
A nested leucine rich repeat (LRR) domain: The precursor of LRRs is a ten or eleven residue motif
TLDR
Proteins having "IRREKO" LRR domain are suggested to adopt an arc shape with smaller curvature in which β-strands are formed on both concave and convex surfaces and that the ancestor of IRREKO@LRR is 10 or 11 residues of LxxLxLxxNx(x/-).
Quantitative analysis and prediction of curvature in leucine‐rich repeat proteins
TLDR
An automated, quantitative protocol is developed that can be used to predict accurately the curvature of leucine‐rich repeat proteins of unknown structure from sequence alone and is demonstrated the effectiveness of this method in selecting a suitable template for comparative modeling.
Leucine-Rich Repeat (LRR) Domains Containing Intervening Motifs in Plants
TLDR
19 families of LRR proteins having non-LRR IRs (LRR@IR proteins) from various plant species are reviewed, finding the rule of N1 » N2 might play a common, significant role in ligand interaction, dimerization, and/or signal transduction of the L RR-RLKs and the LRR-RLPs.
Human leucine-rich repeat proteins: a genome-wide bioinformatic categorization and functional analysis in innate immunity
TLDR
A categorization of 375 human LRR-containing proteins is provided and it is shown that MFHAS1 regulates Toll-like receptor (TLR)–dependent signaling and LRSAM1 is identified as a component of the antibacterial autophagic response.
A Cys-capping motif unique to small leucine-rich repeat proteins and proteoglycans of the extracellular matrix
Proteins with internal repeat structures present particular challenges to methods of classification. Major repeat patterns are straightforward to identify and tend to dominate the annotation of
Comparative sequence analysis of leucine-rich repeats (LRRs) within vertebrate toll-like receptors
TLDR
The super-repeat in the TLR7 family suggests strongly that "bacterial" and "typical" LRRs evolved from a common precursor and is inferred to play a key role in the structure and/or function of their TLRs.
LRRCE: a leucine-rich repeat cysteine capping motif unique to the chordate lineage
TLDR
The search has expanded the family of SLRPs to include new predicted protein sequences, mainly in fishes but with intriguing putative orthologs in mammals, and suggests an early chordate evolutionary origin for the LRRCE capping motif.
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