A capping domain for LRR protein interaction modules.

H Ceulemans; M De Maeyer; W Stalmans; M Bollen

doi:10.1016/s0014-5793(99)00965-5

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PubMed · 10462041

A capping domain for LRR protein interaction modules.

H Ceulemans·M De Maeyer·W Stalmans·M Bollen

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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.

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Amino Acid Sequence Leucine-Rich Repeat Proteins Models, Molecular Molecular Sequence Data Protein Conformation Proteins Repetitive Sequences, Amino Acid Ribonucleoprotein, U2 Small Nuclear Sequence Homology, Amino Acid Journal Article

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H Ceulemans, M De Maeyer, W Stalmans, M Bollen. 1999-08-13. A capping domain for LRR protein interaction modules.. https://doi.org/10.1016/s0014-5793(99)00965-5

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