The leucine-rich repeat: a versatile binding motif.
By Bostjan Kobe, J. Deisenhofer. 1994
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- Shin-Han Shiu
- A. Bleecker
- J. Fahrentrapp
- M. Ascoli
- Giovanni A. L. Broggini
- Minkyung Baek
- S. Fujioka
- J. Dauparas
Citations in the corpus
- Hallucinating symmetric protein assemblies (2022, background): “While the α/β topology of some of these larger HALs is reminiscent of natural Leucine Rich Repeats (LRRs, (34)), which is reflected by a median highest protomer TM-scores of 0.”
- Mutations of gonadotropins and gonadotropin receptors: elucidating the physiology and pathophysiology of pituitary-gonadal function. (2000, background): “found in a diverse group of proteins (13, 14).”
- Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors. (2007, background): “These domains are conserved features among most extracellular LRR proteins (Kobe and Deisenhofer, 1994).”
- Protein repeats: structures, functions, and evolution. (2001, background): “Leucine-rich repeats (Kobe and Deisenhofer, 1994) (LRRs) are relatively short in comparison to other repeat families, with lengths of about 20 amino acids.”
- The lutropin/choriogonadotropin receptor, a 2002 perspective. (2002, background): “Tandem arrays of LRRs have been found in many proteins including hormone receptors and other hormone binding proteins, cell adhesion and extracellular matrix proteins, enzymes, and enzyme inhibitors (42, 43).”
- Plant NBS-LRR proteins in pathogen sensing and host defense (2006, background): “Several LRR domains from non-plant proteins have been crystallized; they form barrel-like structures with a parallel β-sheet lining the inner concave surface and α-helical structures comprising much of the rest of the domai”
- A receptor kinase gene regulating symbiotic nodule development (2002, background): “2a , the predicted proteins possess an amino-terminal signal peptide motif, a putative extracellular domain containing three leucine-rich repeat (LRR) motif”
- MAX1 and MAX2 control shoot lateral branching in Arabidopsis. (2002, background): “MAX2 deviates from a perfect LRR structure (Kobe and Deisenhofer, 1994), as the distance between the repeats varies.”
- Plant Receptor-Like Kinase Gene Family: Diversity, Function, and Signaling (2001, background): “Downstream of the multiprotein signaling complex, two genes, WUSCHEL (16, 90) and POLTERGEIST (91), are negatively regulated by CLAVATA1.”
- Dental adhesion review: aging and stability of the bonded interface. (2008, background): “In other words proteoglycansmay be responsible of the three-dimensional appearance of the dentin organic matrix due to their ability to fill space, bind and organize water molecules, and repel negatively charged molecules [72–76].”
- Hallucinating protein assemblies (2022, background): “While the α/β topology of some of these larger HALs is reminiscent of natural Leucine Rich Repeats (LRRs, ( 31 )), which is reflected by a median highest protomer TM-scores of 0.64, these ring-shaped structures differ considerably from the horseshoe folds of LRRs that do not close into cyclic…”