Structural analysis of leucine-rich-repeat variants in proteins associated with human diseases |
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| Authors: | N. Matsushima N. Tachi Y. Kuroki P. Enkhbayar M. Osaki M. Kamiya R. H. Kretsinger |
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| Affiliation: | (1) Division of Biophysics, School of Health Sciences, Sapporo Medical University, Sapporo, Hokkaido 060-8556, Japan;(2) Department of Occupational Therapy, School of Health Sciences, Sapporo Medical University, Sapporo, Hokkaido 060-8556, Japan;(3) Department of Biochemistry, School of Medicine, Sapporo Medical University, Sapporo, Hokkaido 060-8556, Japan;(4) Department of Biophysics, Faculty of Biology, National University of Mongolia, Ulaanbaatar, 210646/377, Mongolia;(5) Division of Agricultural Science, Graduate School of Agriculture, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan;(6) Division of Biological Science, Graduate School of Science, Hokkaido University, Sapporo, Hokkaido 060-0810, Japan;(7) Department of Biology, University of Virginia, Charlottesville, Virginia 22904, USA |
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| Abstract: | A number of human diseases have been shown to be associated with mutation in the genes encoding leucine-rich-repeat (LRR)-containing proteins. They include 16 different LRR proteins. Mutations of these proteins are associated with 19 human diseases. The mutations occur frequently within the LRR domains as well as their neighboring domains, including cysteine clusters. Here, based on the sequence analysis of the LRR domains and the known structure of LRR proteins, we describe some features of different sequence variants and discuss their adverse effects. The mutations in the cysteine clusters, which preclude the formation of sulfide bridges or lead to a wrong paring of cysteines in extracellular proteins or extracellular domains, occur with high frequency. In contrast, missense mutations at some specific positions in LRRs are very rare or are not observed at all. Received 4 May 2005; received after revision 18 August 2005; accepted 1 September 2005 |
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| Keywords: | Leucine-rich repeats human diseases cysteine clusters typical LRR motif RI-like LRR motif Cryopyrin/Nalp3/PYPAF1 CARD15 |
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