A concanavalin A-like lectin domain in the CHS1/LYST protein, shared by members of the BEACH family.
CHS1/LYST, the causative protein of the Chediak-Higashi syndrome (CHS), belongs to the BEACH (named after BEige And Chediak-Higashi) 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.
Burgess
Agathe
A
INSERM, U768, Paris, F-75015, France.
Mornon
Jean-Paul
JP
de Saint-Basile
Geneviève
G
Callebaut
Isabelle
I
D000595:Amino Acid Sequence; D001665:Binding Sites; D019295:Computational Biology / Q000379:methods*; D003208:Concanavalin A / Q000737:chemistry*; D030562:Databases, Protein; D008969:Molecular Sequence Data; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D033921:Vesicular Transport Proteins / Q000737:chemistry*
C102161:LYST protein, human; D033921:Vesicular Transport Proteins; D003208:Concanavalin A