S.Krauchenco
et al.
(2004).
Three-dimensional structure of an unusual Kunitz (STI) type trypsin inhibitor from Copaifera langsdorffii.
Biochimie,
86,
167-172.
PubMed id: 15134830
DOI: 10.1016/j.biochi.2004.03.004
The crystallographic structure of a novel trypsin inhibitor (CTI) from Copaifera
langsdorffii is reported. The structure was solved by MIRAS procedure and
refined to a crystallographic residual of 17.3% (R(free) = 20.3%) at 1.8 A
resolution. Two isomorphous derivatives were obtained by quick cryo-soaking
approach. CTI is the first structure of a member of Kunitz (STI) family formed
by two noncovalently bound polypeptide chains and only one disulfide bridge. A
standard Kunitz-type inhibitor has a single polypeptide chain and two disulfide
bridges. Structural features granting CTI high inhibitory activity are discussed.