Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
The three-dimensional structure of a novel Kunitz (STI) family member, an inhibitor purified from Delonix regia seeds (DrTI), was solved by molecular replacement method and refined, respectively, to R(factor) and R(free) values of 21.5% and 25.3% at 1.75A resolution. The structure has a classical beta-trefoil fold, however, differently from canonical Kunitz type (STI) inhibitors, its reactive site loop has an insertion of one residue, Glu68, between the residues P1 and P2. Surprisingly, DrTI is an effective inhibitor of trypsin and human plasma kallikrein, but not of chymotrypsin and tissue kallikrein. Putative structural grounds of such specificity are discussed.
Crystal structure of the Kunitz (STI)-type inhibitor from Delonix regia seeds.,Krauchenco S, Pando SC, Marangoni S, Polikarpov I Biochem Biophys Res Commun. 2003 Dec 26;312(4):1303-8. PMID:14652016[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Krauchenco S, Pando SC, Marangoni S, Polikarpov I. Crystal structure of the Kunitz (STI)-type inhibitor from Delonix regia seeds. Biochem Biophys Res Commun. 2003 Dec 26;312(4):1303-8. PMID:14652016
