Structural highlights
Function
VKT1_STIHL Active against serine, cysteine, and aspartic proteases. Can bind vertebrate trypsin and chymotrypsin.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Garcia-Fernandez R, Pons T, Perbandt M, Valiente PA, Talavera A, Gonzalez-Gonzalez Y, Rehders D, Chavez MA, Betzel C, Redecke L. Structural insights into serine protease inhibition by a marine invertebrate BPTI Kunitz-type inhibitor. J Struct Biol. 2012 Sep 5. pii: S1047-8477(12)00240-7. doi:, 10.1016/j.jsb.2012.08.009. PMID:22975140 doi:http://dx.doi.org/10.1016/j.jsb.2012.08.009
- ↑ Delfin J, Martinez I, Antuch W, Morera V, Gonzalez Y, Rodriguez R, Marquez M, Saroyan A, Larionova N, Diaz J, Padron G, Chavez M. Purification, characterization and immobilization of proteinase inhibitors from Stichodactyla helianthus. Toxicon. 1996 Nov-Dec;34(11-12):1367-76. PMID:9027993