alexa Analyses of non-leucine-rich repeat (non-LRR) regions intervening between LRRs in proteins.
Bioinformatics & Systems Biology

Bioinformatics & Systems Biology

Journal of Proteomics & Bioinformatics

Author(s): Matsushima N, Mikami T, Tanaka T, Miyashita H, Yamada K,

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Abstract BACKGROUND: Many proteins have LRR (leucine-rich repeat) units interrupted by non-LRRs which we call IR (non-LRR island region). METHODS: We identified proteins containing [email protected] (LRRs having IR) by using a new method and then analyzed their natures and distributions. RESULTS: [email protected] proteins were found in over two hundred proteins from prokaryotes and from eukaryotes. These are divided into twenty-one different protein families. The IRs occur one to four times in LRR regions and range in length from 5 to 11,265 residues. The IR lengths in Fungi adenylate cyclases (acys) range from 5 to 116 residues; there are 22 LRR repeats. The IRs in Leishmania proteophosphoglycans (ppgs) vary from 105 to 11,265 residues. These results indicate that the IRs evolved rapidly. A group of [email protected] proteins-LRRC17, chondroadherin-like protein, ppgs, and four Pseudomonas proteins-have a super motif consisting of an LRR block and its adjacent [email protected] region. This indicates that the entire super motif experienced duplication. The sequence analysis of IRs offers functional similarity in some [email protected] protein families. GENERAL SIGNIFICANCE: This study suggests that various IRs and super motifs provide a great variety of structures and functions for LRRs. This article was published in Biochim Biophys Acta and referenced in Journal of Proteomics & Bioinformatics

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