Literature DB >> 10462041

A capping domain for LRR protein interaction modules.

H Ceulemans1, M De Maeyer, W Stalmans, M Bollen.   

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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Year:  1999        PMID： 10462041     DOI： 10.1016/s0014-5793(99)00965-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  19 in total

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4.  The leucine-rich repeat domain of Internalin B folds along a polarized N-terminal pathway.

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