A leucine-rich repeat variant with a novel repetitive protein structural motif

@article{Peters1996ALR,
  title={A leucine-rich repeat variant with a novel repetitive protein structural motif},
  author={John W. Peters and Michael H. B. Stowell and Douglas C. Rees},
  journal={Nature Structural Biology},
  year={1996},
  volume={3},
  pages={991-994}
}
The structure of the leucine-rich repeat variant protein reveals a novel fold consisting of alternating α- and 3_(10)-helices arranged in a right-handed superhelix that follows an N-terminal 4Fe:4S cluster-containing domain. 
Leucines on a roll
  • B. Kobe
  • Physics, Biology
    Nature Structural Biology
  • 1996
TLDR
The structure of the leucine-rich repeat variant protein represents an unexpected addition to the list of such proteins, with the repetitive unit consisting of antiparallel alpha- and 3(10)-helices.
Topological characteristics of helical repeat proteins.
The leucine-rich repeat as a protein recognition motif.
The leucine-rich repeat structure
TLDR
An update of the current understanding of leucine-rich repeat structure at the primary, secondary, tertiary and quaternary levels is presented and specific examples from recently determined three-dimensional structures are discussed.
Crystal structure of a Pumilio homology domain.
Over the rainbow to translational control
Structures of the Puf domains from the Drosophila Pum and human Pum1 proteins reveal a novel function for a known structural repeat motif and exciting possibilities for the combinatorial assembly of
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Short alanine-based peptides may form 310-helices and not α-helices in aqueous solution
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The experiments suggest that the more likely peptide geometry is a 310-helix, and single and doubly spin-labelled analogues of alanine-based peptides in which the nitroxide spin label forms an unbranched side chain extending from the sulphur atom of a cysteine residue are designed.
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TLDR
The crystal structure of the nitrogenase Fe-protein from Azotobacter vinelandii has been determined and it appears that interactions between the nucleotide and cluster sites must be indirectly coupled by allosteric changes occurring at the subunit interface.
A program to produce both detailed and schematic plots of protein structures
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