title: A capping domain for LRR protein interaction modules.
abstract: Leucine-rich repeats (LRR) are protein interaction modules which are present in a large number of proteins with diverse functions. We describe here a novel motif (16-19 residues) downstream of the last, incomplete, LRR in a subfamily of LRR proteins. In the U2A' spliceosomal protein, this motif is folded into a cap that shields the hydrophobic core of the LRRs from the solvent. Modelling of the LRR-cap in the imidazoline-1 candidate receptor, using the known structure of U2A' as template, showed a conservation of the basic structural features.
authors.affiliation: Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit Leuven, Belgium.
authors.forename: H
authors.initials: H
authors.lastname: Ceulemans
authors.forename: M
authors.initials: M
authors.lastname: De Maeyer
authors.forename: W
authors.initials: W
authors.lastname: Stalmans
authors.forename: M
authors.initials: M
authors.lastname: Bollen
mesh_terms: D000595:Amino Acid Sequence; D000090263:Leucine-Rich Repeat Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D020449:Repetitive Sequences, Amino Acid; D017413:Ribonucleoprotein, U2 Small Nuclear / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
chemical_list: D000090263:Leucine-Rich Repeat Proteins; D011506:Proteins; D017413:Ribonucleoprotein, U2 Small Nuclear