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6LF5

The solution structure of ShSPI

Summary for 6LF5
Entry DOI10.2210/pdb6lf5/pdb
DescriptorShSPI (1 entity in total)
Functional Keywordsneutrophil elastase inhibitor, toxin
Biological sourceScolopendra hainanum
Total number of polymer chains1
Total formula weight3960.59
Authors
Luan, N.,Rong, M.Q.,Liu, J.X.,Lai, R. (deposition date: 2019-11-29, release date: 2020-12-02, Last modification date: 2024-10-23)
Primary citationLuan, N.,Zhao, Q.,Duan, Z.,Ji, M.,Xing, M.,Zhu, T.,Mwangi, J.,Rong, M.,Liu, J.,Lai, R.
Identification and Characterization of ShSPI, a Kazal-Type Elastase Inhibitor from the Venom of Scolopendra Hainanum .
Toxins, 11:-, 2019
Cited by
PubMed Abstract: Elastase 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 . ShSPI showed significant inhibitory effects on porcine pancreatic elastase and human neutrophils elastase with 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.
PubMed: 31817486
DOI: 10.3390/toxins11120708
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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