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Publication Abstract from PubMed

Kunitz type trypsin inhibitors bind to the active pocket of trypsin causing its inhibition. Plant Kunitz type inhibitors are thought to be important in defense, especially against insect pests. From sequence analysis of various Kunitz type inhibitors from plants, we identified CaTI2 from chickpea as a unique variant lacking the functionally important arginine residue corresponding to the Soybean trypsin inhibitor (STI) and having a distinct and unique inhibitory loop organization. To further explore the implications of these sequence variations, we obtained the crystal structure of recombinant CaTI2 at 2.8A resolution. It is evident from the structure that the variations in the inhibitory loop facilitates non-substrate like binding of CaTI2 to trypsin, while the canonical inhibitor STI binds to trypsin in substrate like manner. Our results establish the unique mechanism of trypsin inhibition by CaTI2, which warrant further research into its substrate spectrum.

Structural insights into the unique inhibitory mechanism of Kunitz type trypsin inhibitor from Cicer arietinum L.,Bendre AD, Suresh CG, Shanmugam D, Ramasamy S J Biomol Struct Dyn. 2018 Jul 27:1-38. doi: 10.1080/07391102.2018.1494633. PMID:30052127^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.