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Article

Experimental and theoretical evidence supporting the role of Gly363 in blood coagulation factor IXa (Gly193 in chymotrypsin) for proper activation of the proenzyme.

The Journal of biological chemistry - 15 Feb 1990

Bajaj S P, Spitzer S G, Welsh W J, Warn-Cramer B J, Kasper C K, Birktoft J J

Abstract excerpt

Factor IX is the zymogen of the serine protease factor IXa involved in blood coagulation. In addition to a catalytic domain homologous to the chymotrypsin family, it has Ca2+, phospholipid, and factor VIIIa binding regions needed for full biologic activity. We isolated a nonfunctional factor IX protein designated factor IXEagle Rock (IXER) from a patient with hemophilia B. The variant protein is indistinguishable...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 2303434

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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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Experimental and theoretical evidence supporting the role of Gly363 in blood coagulation factor IXa (Gly193 in chymotrypsin) for proper activation of the proenzyme.PMID 2303434Read ↗

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Protease and EGF1 domains of factor IXa play distinct roles in binding to factor VIIIa. Importance of helix 330 (helix 162 in chymotrypsin) of protease domain of factor IXa in its interaction with factor VIIIa.Semantic proximity Read ↗

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A frequent human coagulation Factor VII mutation (A294V, c152) in loop 140s affects the interaction with activators, tissue factor and substrates.Semantic proximity Read ↗

Expression, purification and characterization of factor IX derivatives using a novel vector system.Semantic proximity Read ↗

Analysis of the factor XI variant Arg184Gly suggests a structural basis for factor IX binding to factor XIa.Semantic proximity Read ↗

The distinct roles that Gln-192 and Glu-217 of factor IX play in selectivity for macromolecular substrates and inhibitors.Semantic proximity Read ↗

Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX.Semantic proximity Read ↗

A recurrent Gly43Asp substitution in coagulation Factor X rigidifies its catalytic pocket and impairs catalytic activity and intracellular trafficking.Semantic proximity Read ↗

Coagulation factor XII protease domain crystal structure.Semantic proximity Read ↗

Interaction of factor IXa with factor VIIIa. Effects of protease domain Ca2+ binding site, proteolysis in the autolysis loop, phospholipid, and factor X.Semantic proximity Read ↗

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