Journal
BIOINFORMATICS
Volume 25, Issue 10, Pages 1219-1222Publisher
OXFORD UNIV PRESS
DOI: 10.1093/bioinformatics/btp151
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CHS1/LYST, the causative protein of the Chediak-Higashi syndrome (CHS), belongs to the BEACH (named after BEige And ChediakHigashi) family, which includes various large proteins sharing the same C-terminal domain architecture [a PH (Pleckstrin homology)BEACH domain followed by WD repeats). Members of the BEACH family are generally defined as vesicle-trafficking regulatory proteins, but their functions remain to be determined at the molecular level. Here, using a panel of sensitive methods of sequence analysis, we show that the N-terminal regions of BEACH proteins contain an as yet not described domain, which shares striking similarities with clostridial neurotoxins and defines a novel family within the concanavalin A (ConA)-like lectin superfamily. These results suggest that the BEACH ConA-like lectin domain could be involved in oligosaccharide binding associated with protein traffic and sorting along the secretory pathway, especially in relation with components of the vesicle fusion machinery.
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