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Article

The role of the protein core in the inhibitory power of the classic serine protease inhibitor, chymotrypsin inhibitor 2.

Biochemistry - 3 Jun 2003

Radisky Evette S, King David S, Kwan Gene, Koshland Daniel E

Abstract excerpt

A synthetic cyclic peptide, reported to be a tight-binding inhibitor of serine proteases, is instead found to be a good substrate, as is the linear peptide of the same sequence. Both of the peptides, designed to mimic the binding loop of chymotrypsin inhibitor 2 (CI2), were cleaved by subtilisin primarily at the CI2 reactive-site Met-59-Glu-60 bond, revealing that the sequence, in the absence of the structural...

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Identifiers

PMID: 12767231
DOI: 10.1021/bi034275d

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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