Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Three-dimensional structure of an unusual Kunitz (STI) type trypsin inhibitor from Copaifera langsdorffii.,Krauchenco S, Nagem RA, da Silva JA, Marangoni S, Polikarpov I Biochimie. 2004 Mar;86(3):167-72. PMID:15134830[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Krauchenco S, Nagem RA, da Silva JA, Marangoni S, Polikarpov I. Three-dimensional structure of an unusual Kunitz (STI) type trypsin inhibitor from Copaifera langsdorffii. Biochimie. 2004 Mar;86(3):167-72. PMID:15134830 doi:10.1016/j.biochi.2004.03.004