Search for fucose binding domains in recently sequenced hypothetical proteins using molecular modeling techniques and structural analysis.

The crystal structure of a fucose-binding lectin from the bacteria Pseudomonas aeruginosa in complex with alpha-L-fucose has been recently determined. It is a tetramer; each monomer displays a nine-stranded, antiparallel, beta-sandwiched arrangement and contains two calcium ions that mediate the binding of fucose in a recognition mode unique among protein-carbohydrate interactions. In search of this type of unique interactions in other newly discovered protein sequences, we have used molecular modeling techniques to predict and analyze the 3-D structures of some proteins, which exhibited reasonable degree of homology with the amino acid sequence of the bacterial protein.

Structural studies on mannose-selective glycoprotein receptors using molecular modeling techniques.

Glycoproteins play important roles in various cellular events and their presence in appropriate locations in proper active conformations is essential for many biochemical functions. Recent evidences suggest that some glycoproteins may require sorting receptors for efficient exit from the endoplasmic reticulum. These receptors need the presence of calcium or other metal ions for their native activity.