A capping domain for LRR protein interaction modules

FEBS Letters

De Maeyer, Marc²  Bollen, Mathieu¹  Ceulemans, Hugo¹  Stalmans, Willy¹ 

[1] Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit Leuven, Leuven, Belgium;Centrum voor Transgene Technologie en Gentherapie (VIB), Herestraat 49, B-3000 Leuven, Belgium

关键词: Leucine-rich repeat;    sds22;   

DOI  :  10.1016/S0014-5793(99)00965-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown