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Article

Residue Met(156) contributes to the labile enzyme conformation of coagulation factor VIIa.

The Journal of biological chemistry - 2 Mar 2001

Petrovan R J, Ruf W

Abstract excerpt

Serine protease activation is typically controlled by proteolytic cleavage of the scissile bond, resulting in spontaneous formation of the activating Ile(16)-Asp(194) salt bridge. The initiating coagulation protease factor VIIa (VIIa) differs by remaining in a zymogen-like conformation that confe...

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Identifiers

PMID: 11078728
DOI: 10.1074/jbc.M004726200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11078728-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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Residue Met(156) contributes to the labile enzyme conformation of coagulation factor VIIa.PMID 11078728Read ↗

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