A capping domain for LRR protein interaction modules

被引：32

作者：

Ceulemans, H

De Maeyer, M

Stalmans, W

Bollen, M ^{[1
]}

机构：

[1] Katholieke Univ Leuven, Fac Geneeskunde, Afdeling Biochem, Louvain, Belgium

[2] VIB, Centrum Transgene Technol & Gentherapie, B-3000 Louvain, Belgium

来源：

FEBS LETTERS | 1999年 / 456卷 / 03期

关键词：

leucine-rich repeat; sds22;

D O I：

10.1016/S0014-5793(99)00965-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Leucine-rich repeats (LRR) are protein interaction modules which are present in a large number of proteins with diverse functions. Wt 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. (C) 1999 Federation of European Biochemical Societies.

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页码：349 / 351

页数：3

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