A leucine‐rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a β‐sheet structure

@article{Gay1991ALR,
  title={A leucine‐rich repeat peptide derived from the Drosophila Toll receptor forms extended filaments with a $\beta$‐sheet structure},
  author={Nicholas J. Gay and Len C. Packman and Mike Weldon and Jennifer C. J. Barna},
  journal={FEBS Letters},
  year={1991},
  volume={291}
}
The leucine-rich repeat: a versatile binding motif.
A minimum folding unit in the ankyrin repeat protein p16(INK4).
The ankyrin repeat is an abundant, 33 residue sequence motif that forms a consecutive beta-hairpin-helix-loop-helix (beta(2)alpha(2)) fold. Most ankyrin repeat proteins consist of four or more
Fission Yeast Leucine-Rich Repeat Protein Lrp1 Is Essential for Cell Morphogenesis as a Component of the Morphogenesis Orb6 Network (MOR)
TLDR
It is shown that the conserved leucine-rich repeat protein Lrp1 is required for cell morphogenesis as a newly recognized component of MOR, and proved to function upstream of Orb6 in cell Morphogenesis.
Polycystin: new aspects of structure, function, and regulation.
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  • Biology
    Journal of the American Society of Nephrology : JASN
  • 2001
TLDR
It is proposed that polycystin-1 functions as a matrix receptor to link the extracellular matrix to the actin cytoskeleton via focal adhesion proteins and genetic evidence suggests that PKD1, PKD2, NPHP1, and tensin are in the same pathway.
Unusually stable β‐sheet formation in an ionic self‐complementary oligopeptide
A 16‐residue amphiphilic oligopeptide (EAK16) with every other residue alanine and also containing glutamic acid and lysine (Ac‐NH‐AEAEAKAKAEAEAKAK‐CONH2) is able to form an unusually stable β‐sheet
Pulmonary surfactant‐associated polypeptide C in a mixed organic solvent transforms from a monomeric α‐helical state into insoluble β‐sheet aggregates
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The α‐helical form of SP‐C seems to be the thermodynamically most stable state in this micellar environment, whereas its presence in freshly prepared samples in a mixed solvent is due to a high kinetic barrier for unfolding.
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The Drosophila membrane receptor Toll can function to promote cellular adhesion.
TLDR
The presence in Toll protein of additional sequences held in common with the human membrane receptor platelet glycoprotein 1b (Gp1b) are reported, suggesting that the biochemical function of Toll protein is more closely analogous to that of Gp1B than previously thought.
The primary structure of human ribonuclease/angiogenin inhibitor (RAI) discloses a novel highly diversified protein superfamily with a common repetitive module.
TLDR
It is proposed that these repetitive modules are a common structural feature of a novel protein superfamily whose members exert their function by highly specific protein‐protein interactions.
Drosophila chaoptin, a member of the leucine‐rich repeat family, is a photoreceptor cell‐specific adhesion molecule.
TLDR
Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl‐phosphatidylinositol.
The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence.
The primary structure of the beta chain of human glycoprotein Ib (GPIb), the platelet receptor for von Willebrand factor, has been established by a combination of cDNA cloning and amino acid sequence
Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein.
TLDR
The amino acid sequence of the alpha chain of GPIb predicted from the cDNA agreed completely with the sequence of 156 amino acids that was determined by Edman degradation of peptides isolated from human platelet glycocalicin after digestion with trypsin or Staphylococcus aureus V8 protease.
Leucine-rich repeats and carboxyl terminus are required for interaction of yeast adenylate cyclase with RAS proteins.
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TLDR
It is found that the fusion containing both the NH2-terminal 1600 residues and the COOH- terminus of the Sa.
Lutropin-choriogonadotropin receptor: an unusual member of the G protein-coupled receptor family.
TLDR
The LH-CG-R gene may have evolved by recombination of LRG and G protein-coupled receptor genes and bind human choriogonadotropin with high affinity and show an increase in cyclic adenosine monophosphate when exposed to hormone.
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