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A capping domain for LRR protein interaction modules
Author(s) -
Ceulemans Hugo,
De Maeyer Marc,
Stalmans Willy,
Bollen Mathieu
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00965-5
Subject(s) - leucine rich repeat , computational biology , subfamily , protein structure , biology , genetics , chemistry , biochemistry , receptor , gene
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.