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Article

Role of the I16-D194 ionic interaction in the trypsin fold.

Scientific reports - 2 Dec 2019

Stojanovski Bosko M, Chen Zhiwei, Koester Sarah K, Pelc Leslie A, Di Cera Enrico

Abstract excerpt

Activity in trypsin-like proteases is the result of proteolytic cleavage at R15 followed by an ionic interaction that ensues between the new N terminus of I16 and the side chain of the highly conserved D194. This mechanism of activation, first proposed by Huber and Bode, organizes the oxyanion hole and primary specificity pocket for substrate binding and catalysis. Using the clotting protease thrombin as a...

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Identifiers

PMID: 31792294
DOI: 10.1038/s41598-019-54564-6
PMCID: PMC6889508

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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