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

Identification of residues in the 558-loop of factor VIIIa A2 subunit that interact with factor IXa.

The Journal of biological chemistry - 20 Nov 2009

Jagannathan Indu, Ichikawa H Travis, Kruger Tricia, Fay Philip J

Abstract excerpt

Factor VIIIa is comprised of A1, A2, and A3C1C2 subunits. Several lines of evidence have identified the A2 558-loop as interacting with factor IXa. The contributions of individual residues within this region to inter-protein affinity and cofactor activity were assessed following alanine scanning mutagenesis of residues 555-571 that border or are contained within the loop. Variants were expressed as isolated A2...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Catalysis
Share to Cricetinae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Enzyme Inhibitors

Share to Insecta

Share to Kinetics

Share to Mutagenesis

Source

Open in PubMed Open full text

Identifiers

PMID: 19801661
DOI: 10.1074/jbc.M109.050781
PMCID: PMC2781637

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of residues in the 558-loop of factor VIIIa A2 subunit that interact with factor IXa.PMID 19801661Read ↗

Enhanced factor VIIIa stability of A2 domain interface variants results from an increased apparent affinity for the A2 subunit. Results from an increased apparent affinity for the A2 subunit.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 ↗

Modification of interdomain interfaces within the A3C1C2 subunit of factor VIII affects its stability and activity.Semantic proximity Read ↗

Functional mapping of the A2 domain from human factor VIII.Semantic proximity Read ↗

Cofactor activity in factor VIIIa of the blood clotting pathway is stabilized by an interdomain bond between His281 and Ser524 formed in factor VIII.Semantic proximity Read ↗

Identification of amino acid residues that are crucial for FXIII-A intersubunit interactions and stability.Semantic proximity Read ↗

Stabilizing interactions between D666-S1787 and T657-Y1792 at the A2-A3 interface support factor VIIIa stability in the blood clotting pathway.Semantic proximity Read ↗

Identification of residues contributing to A2 domain-dependent structural stability in factor VIII and factor VIIIa.Semantic proximity Read ↗

Increasing hydrophobicity or disulfide bridging at the factor VIII A1 and C2 domain interface enhances procofactor stability.Semantic proximity Read ↗

Computational analysis of Asp519 and Glu665 mutations of coagulation factor FVIIIa: Implications for enhanced binding affinity of A2-domain.Semantic proximity Read ↗

Contribution of Factor VIII A2 Domain Residues 400-409 to a Factor X-Interactive Site in the Factor Xase Complex.Semantic proximity Read ↗

Functional mapping of factor VIII C2 domain.Semantic proximity Read ↗

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