Abstract:
: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.
journal_name
Biochimiejournal_title
Biochimieauthors
Krauchenco S,Nagem RA,da Silva JA,Marangoni S,Polikarpov Idoi
10.1016/j.biochi.2004.03.004keywords:
subject
Has Abstractpub_date
2004-03-01 00:00:00pages
167-72issue
3eissn
0300-9084issn
1638-6183pii
S0300908404000367journal_volume
86pub_type
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