Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Journal of biological chemistry - 12 Sept 1997

Mathur A, Zhong D, Sabharwal A K, Smith K J, Bajaj S P

Abstract excerpt

We previously identified a high affinity Ca2+ binding site in the protease domain of factor IXa involving Glu235 (Glu70 in chymotrypsinogen numbering; hereafter, the numbers in brackets refer to the chymotrypsin equivalents) and Glu245[80] as putative ligands. To delineate the function of this Ca2+ binding site, we expressed IXwild type (IXWT), IXE235K, and IXE245V in 293 kidney cells and compared their...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding, Competitive
Share to Binding Sites

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

Share to Calcium

Share to Enzyme Activation

Share to Models, Molecular

Share to Mutation

Share to Peptide Fragments

Share to Protein Binding

Source

Identifiers

PMID: 9287357
DOI: 10.1074/jbc.272.37.23418

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interaction of factor IXa with factor VIIIa. Effects of protease domain Ca2+ binding site, proteolysis in the autolysis loop, phospholipid, and factor X.PMID 9287357Read ↗

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 ↗

Mutations associated with hemophilia A in the 558-565 loop of the factor VIIIa A2 subunit alter the catalytic activity of the factor Xase complex.Semantic proximity Read ↗

A sequential mechanism for exosite-mediated factor IX activation by factor XIa.Semantic proximity Read ↗

Asp-70-->Lys mutant of factor X lacks high affinity Ca2+ binding site yet retains function.Semantic proximity Read ↗

Comparative platelet binding and kinetic studies with normal and variant factor IXa molecules.Semantic proximity Read ↗

Ca2+ Binding to the First Epidermal Growth Factor-like Domain of Human Blood Coagulation Factor IX Promotes Enzyme Activity and Factor VIII Light Chain BindingSemantic proximity Read ↗

Identification of residues Asn89, Ile90, and Val107 of the factor IXa second epidermal growth factor domain that are essential for the assembly of the factor X-activating complex on activated platelets.Semantic proximity Read ↗

The first epidermal growth factor-like domains of factor Xa and factor IXa are important for the activation of the factor VII--tissue factor complex.Semantic proximity Read ↗

An important role for the activation peptide domain in controlling factor IX levels in the blood of haemophilia B mice.Semantic proximity Read ↗

Factor IX Bm Kiryu: a Val-313-to-Asp substitution in the catalytic domain results in loss of function due to a conformational change of the surface loop: evidence obtained by chimaeric modelling.Semantic proximity Read ↗

The activation peptide of coagulation factor XIII is vital for its expression and stability.Semantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.