title: Artificial leucine rich repeats as new scaffolds for protein design.
abstract: The leucine rich repeat (LRR) motif that participates in many biomolecular recognition events in cells was suggested as a general scaffold for producing artificial receptors. We describe here the design and first total chemical synthesis of small LRR proteins, and their structural analysis. When evaluating the tertiary structure as a function of different number of repeating units (1-3), we were able to find that the 3-repeats sequence, containing 90 amino acids, folds into the expected structure.
authors.affiliation: Department of Chemistry, Ben Gurion University of the Negev, Beer Sheva, Israel.
authors.forename: Hemda
authors.initials: H
authors.lastname: Baabur-Cohen
authors.forename: Subashini
authors.initials: S
authors.lastname: Dayalan
authors.forename: Inbal
authors.initials: I
authors.lastname: Shumacher
authors.forename: Rivka
authors.initials: R
authors.lastname: Cohen-Luria
authors.forename: Gonen
authors.initials: G
authors.lastname: Ashkenasy
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D002942:Circular Dichroism; D007930:Leucine / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D015202:Protein Engineering; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D011506:Proteins; C095768:inlB protein, Listeria monocytogenes; D007930:Leucine