title: Solution structure of a variant of human pancreatic secretory trypsin inhibitor determined by nuclear magnetic resonance spectroscopy.
abstract: The structure of a variant of human pancreatic secretory trypsin inhibitor (PSTI) has been determined by 1H nuclear magnetic resonance (n.m.r.) spectroscopy and a combination of distance geometry and molecular dynamics simulations. After complete assignment of the 1H signals, the nuclear Overhauser data imply the existence of a rather well-determined tertiary structure stabilized by a central alpha-helix and a short three-stranded beta-sheet. The tertiary structure of the amino terminus and of the loop 11-17 could not be defined by n.m.r. data, suggesting a high flexibility in these areas. As the crystal structures of two complexes of human PSTI variants and that of an uncomplexed variant are also known a comparison of the PSTI tertiary structure in solution and in the crystal is now possible.
authors.affiliation: Gesellschaft für Biotechnologische Forschung, Molekulare Strukturforschung, Braunschweig, Germany.
authors.forename: W
authors.initials: W
authors.lastname: Klaus
authors.forename: D
authors.initials: D
authors.lastname: Schomburg
mesh_terms: D000595:Amino Acid Sequence; D003198:Computer Simulation; D006801:Humans; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012984:Software; D012996:Solutions; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000737:chemistry*
chemical_list: D012996:Solutions; D014359:Trypsin Inhibitor, Kazal Pancreatic