Structural highlights
FunctionVKT1_STIHL Active against serine, cysteine, and aspartic proteases. Can bind vertebrate trypsin and chymotrypsin.[1] [2] Publication Abstract from PubMedThe BPTI/Kunitz-type inhibitor family includes several extremely potent serine protease inhibitors. To date, the inhibitory mechanisms have only been studied for mammalian inhibitors. Here, the first crystal structure of a BPTI/Kunitz-type inhibitor from a marine invertebrate (rShPI-1A) is reported to 2.5 A resolution. Crystallization of recombinant rShPI-1A required the salt-induced dissociation of a trypsin complex that was previously formed to avoid intrinsic inhibitor aggregates in solution. The rShPI-1A structure is similar to the NMR structure of the molecule purified from the natural source, but allowed the assignment of disulfide-bridge chiralities and the detection of an internal stabilizing water network. A structural comparison with other BPTI/Kunitz-type canonical inhibitors revealed unusual varphi angles at positions 17 and 30 to be a particular characteristic of the family. A significant clustering of varphi and psi angle values in the glycine-rich remote fragment near the secondary binding loop was additionally identified, but its impact on the specificity of rShPI-1A and similar molecules requires further study. Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus.,Garcia-Fernandez R, Pons T, Meyer A, Perbandt M, Gonzalez-Gonzalez Y, Gil D, de los Angeles Chavez M, Betzel C, Redecke L Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1289-93., doi: 10.1107/S1744309112039085. Epub 2012 Oct 26. PMID:23143234[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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