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|2001 ||Rosengren, K. J., Daly, N. L., Scanlon, M. J. and Craik, D. J. (2001) Solution structure of BSTI: A new trypsin inhibitor from skin secretions of Bombina bombina. Biochemistry, 40 15: 4601-4609.|
The three-dimensional solution structure of BSTI, a trypsin inhibitor from the European frog Bombina bombina, has been solved using H-1 NMR spectroscopy. The 60 amino acid protein contains five disulfide bonds, which were unambiguously determined to be Cvs (4-38), Cys (13-34), Cys (17-30), Cys (21-60), and Cys (40-54) by experimental restraints and subsequent structure calculations. The main elements of secondary structure are four beta -strands, arranged as two small antiparallel beta -sheets, The overall fold of BSTI is disk shaped and is characterized by the lack of a hydrophobic core. The presumed active site is located on a loop comprising residues 21-34, which is a relatively disordered region similar to that seen in many other protease inhibitors. However, the overall fold is different to other known protease inhibitors with the exception of a small family of inhibitors isolated from nematodes of the family Ascaris and recently also from the haemolymph of Apis mellifera. BSTI may thus be classified as a new member of this recently discovered family of protease inhibitors.
| Dr Johan Rosengren, Dr Norelle Daly, Professor David Craik|
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|Links: ||Link to Full Text (DOI)|
|Keywords: ||Biochemistry & Molecular Biology, Nuclear-magnetic-resonance, Nmr Structure Calculation, Torsion Angle Dynamics, Xenopus-laevis, Protease Inhibitors, Molecular-structure, Elastase Inhibitor, Apis-mellifera, Amphibian Skin, Eglin-c|