Homology modeling of the cellulose-binding domain of a pollen allergen from rye grass: structural basis for the cellulose recognition and associated allergenic properties.
A three-dimensional model of the cellulose-binding domain of the rye-grass pollen allergen Lol pI built by homology modeling is proposed as a structural scaffold for expansins and other expansin-related proteins. A groove and an extended strip of aromatic and polar residues presumably account for the cellulose-binding properties of the protein domain. Two of the four predicted T-cell epitopes readily exposed on the surface of the cellulose-binding domain match with previously reported IgE-binding regions. A close structural relationship occurs between the cellulose-binding and allergenic properties.
Institut de Pharmacologie et Biologie Structurale, UMR-CNRS 5089, 205 Route de Narbonne, 31077 4, Toulouse Cedex, France.
Annick
A
Barre
Pierre
P
Rougé
D000485:Allergens / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D000595:Amino Acid Sequence; D052179:Antigens, Plant; D001665:Binding Sites; D002482:Cellulose / Q000378:metabolism*; D018984:Epitopes, T-Lymphocyte / Q000737:chemistry / Q000378:metabolism; D007073:Immunoglobulin E / Q000276:immunology; D008129:Lolium / Q000276:immunology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000276:immunology* / Q000378:metabolism; D011058:Pollen / Q000276:immunology*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D000485:Allergens; D052179:Antigens, Plant; D018984:Epitopes, T-Lymphocyte; C042814:Lol p I protein, Lolium perenne; D010940:Plant Proteins; D007073:Immunoglobulin E; D002482:Cellulose