6lf5 | pdb_00006lf5
The solution structure of ShSPI
Structural highlights
Publication Abstract from PubMedElastase is a globular glycoprotein and belongs to the chymotrypsin family. It is involved in several inflammatory cascades on the basis of cleaving the important connective tissue protein elastin, and is strictly regulated to a balance by several endogenous inhibitors. When elastase and its inhibitors are out of balance, severe diseases will develop, especially those involved in the cardiopulmonary system. Much attention has been attracted in seeking innovative elastase inhibitors and various advancements have been taken on clinical trials of these inhibitors. Natural functional peptides from venomous animals have been shown to have anti-protease properties. Here, we identified a kazal-type serine protease inhibitor named ShSPI from the cDNA library of the venom glands of Scolopendra hainanum. ShSPI showed significant inhibitory effects on porcine pancreatic elastase and human neutrophils elastase with Ki values of 225.83 +/- 20 nM and 12.61 +/- 2 nM, respectively. Together, our results suggest that ShSPI may be an excellent candidate to develop a drug for cardiopulmonary diseases. Identification and Characterization of ShSPI, a Kazal-Type Elastase Inhibitor from the Venom of Scolopendra Hainanum.,Luan N, Zhao Q, Duan Z, Ji M, Xing M, Zhu T, Mwangi J, Rong M, Liu J, Lai R Toxins (Basel). 2019 Dec 5;11(12). pii: toxins11120708. doi:, 10.3390/toxins11120708. PMID:31817486[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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