Solution structure of a variant of human pancreatic secretory trypsin inhibitor determined by nuclear magnetic resonance spectroscopy.
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.
Klaus
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Gesellschaft für Biotechnologische Forschung, Molekulare Strukturforschung, Braunschweig, Germany.
Schomburg
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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*
D012996:Solutions; D014359:Trypsin Inhibitor, Kazal Pancreatic