Complex formation by bovine trypsin and a tetrapeptide (Leu-Arg-Pro-Gly-NH2): X-ray structure analysis of the complex in the orthorhombic crystal form with low molecular packing density.
The title tetrapeptide, Leu-Arg-Pro-Gly-NH2, forms a complex with trypsin in a novel orthorhombic crystal form with low molecular packing density. The complex formation was directly evidenced by X-ray crystallography. The crystal structure at 1.8 A resolution was refined to an R-factor of 20.5% for 13,923 reflection data, which were measured with synchrotron radiation. The tetrapeptide is bound to trypsin at the active site, and the binding mode is very similar to that of a bovine pancreatic trypsin inhibitor (BPTI):trypsin complex. The tetrapeptide:trypsin complex is the first observation that a peptide forms a stable complex with trypsin.
Matsumoto
O
O
Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Taga
T
T
Higashi
T
T
Matsushima
M
M
Machida
K
K
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D014357:Trypsin / Q000737:chemistry*; D014961:X-Ray Diffraction
D009842:Oligopeptides; C068451:leucyl-arginyl-prolyl-glycinamide; D014357:Trypsin