title: Polypeptide chains with similar amino acid sequences but a distinctly different conformation. Bovine and porcine phospholipase A2.
abstract: The primary structures of bovine and porcine pancreatic phospholipase A2 differ only by about 15%. Nevertheless, a 12 residue loop, with only one substitution (Val leads to Phe) has a quite different conformation, whereas the rest of the molecules have a very similar folding indeed. From this observation it is concluded that prediction of a 3-dimensional structure on the basis of sequence similarity of short segments alone might give erroneous results.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D008958:Models, Molecular; D010179:Pancreas / Q000201:enzymology; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D011487:Protein Conformation; D013045:Species Specificity; D013329:Structure-Activity Relationship; D013552:Swine
chemical_list: D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2