title: Fibronectin: multiple interactions assigned to structural domains.
abstract: Characteristic features of fibronectin are its various molecular and biological interactions and a wide distribution in vivo. Structural studies of the protein have indicated that the functions correspond to specific interactive domains in the molecule and have revealed unique, internally homologous sequences in the primary structure. Fibronectin is easily degraded by proteinases and many of its biological effects are shared by the proteolytic fragments which also seem to have effects of their own.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D002241:Carbohydrates / Q000032:analysis; D002352:Carrier Proteins / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D003094:Collagen / Q000378:metabolism; D005353:Fibronectins / Q000032:analysis / Q000378:metabolism / Q000502:physiology; D005780:Gelatin / Q000378:metabolism; D008970:Molecular Weight; D010710:Phosphates / Q000032:analysis; D011487:Protein Conformation; D013438:Sulfhydryl Compounds / Q000032:analysis
chemical_list: D000596:Amino Acids; D002241:Carbohydrates; D002352:Carrier Proteins; D005353:Fibronectins; D010710:Phosphates; D013438:Sulfhydryl Compounds; C033135:gelatin binding protein; D005780:Gelatin; D003094:Collagen