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Article

Dimer dissociation and unfolding mechanism of coagulation factor XI apple 4 domain: spectroscopic and mutational analysis.

Journal of molecular biology - 23 Mar 2007

Riley Paul W, Cheng Hong, Samuel Dharmaraj, Roder Heinrich, Walsh Peter N

Abstract excerpt

The blood coagulation protein factor XI (FXI) consists of a pair of disulfide-linked chains each containing four apple domains and a catalytic domain. The apple 4 domain (A4; F272-E362) mediates non-covalent homodimer formation even when the cysteine involved in an intersubunit disulfide is mutated to serine (C321S). To understand the role of non-covalent interactions stabilizing the FXI dimer, equilibrium...

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Identifiers

PMID: 17257616
DOI: 10.1016/j.jmb.2006.12.066
PMCID: PMC1945241

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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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