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|Title:||Crystallization of a nonclassical Kazal-type Carcinoscorpius rotundicauda serine protease inhibitor, CrSPI-1, complexed with subtilisin|
Kazal-type serine protease inhibitors
|Citation:||Tulsidas, S.R., Thangamani, S., Ho, B., Sivaraman, J., Ding, J.L. (2009). Crystallization of a nonclassical Kazal-type Carcinoscorpius rotundicauda serine protease inhibitor, CrSPI-1, complexed with subtilisin. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 65 (5) : 533-535. ScholarBank@NUS Repository. https://doi.org/10.1107/S1744309109014420|
|Abstract:||Serine proteases play a major role in host-pathogen interactions. The innate immune system is known to respond to invading pathogens in a nonspecific manner. The serine protease cascade is an essential component of the innate immune system of the horseshoe crab. The serine protease inhibitor CrSPI isoform 1 (CrSPI-1), a unique nonclassical Kazal-type inhibitor of molecular weight 9.3 kDa, was identified from the hepatopancreas of the horseshoe crab Carcinoscorpius rotundicauda. It potently inhibits subtilisin and constitutes a powerful innate immune defence against invading microbes. Here, the cloning, expression, purification and cocrystallization of CrSPI-1 with subtilisin are reported. The crystals diffracted to 2.6 Å resolution and belonged to space group P21, with unit-cell parameters a = 73.8, b = 65.0, c = 111.9 Å, Β = 95.4°. The Matthews coefficient (V M = 2.64 Å3 Da-1, corresponding to 53% solvent content) and analysis of the preliminary structure solution indicated the presence of one heterotrimer (1:2 ratio of CrSPI-1:subtilisin) and one free subtilisin molecule in the asymmetric unit. © 2009 International Union of Crystallography. All right reserved.|
|Source Title:||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Appears in Collections:||Staff Publications|
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