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

Probing the molecular basis of factor Xa specificity by mutagenesis of the serpin, antithrombin.

Biochimica et biophysica acta - 3 Oct 2001

Rezaie A R, Yang L

Abstract excerpt

The molecular basis of the substrate and inhibitor specificity of factor Xa, the serine proteinase of the prothrombinase complex, was investigated by constructing two mutants of human antithrombin (HAT) in which the reactive site loop of the serpin from the P4-P4' site was replaced with the corresponding residues of the two factor Xa cleavage sites in prothrombin (HAT/Proth-1 and HAT/Proth-2). These mutants...

Read the complete abstract on PubMed

Topics

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

Share to Antithrombins
Share to Enzyme Precursors
Share to Factor V

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Factor Xa

Share to Genetic Vectors

Share to Heparin

Share to Peptide Fragments

Share to Prothrombin

Source

Identifiers

PMID: 11687304
DOI: 10.1016/s0304-4165(01)00189-1

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Probing the molecular basis of factor Xa specificity by mutagenesis of the serpin, antithrombin.PMID 11687304Read ↗

Evolution of serpin specificity: cooperative interactions in the reactive-site loop sequence of antithrombin specifically restrict the inhibition of activated protein C.Semantic proximity Read ↗

Proexosite-1 on prothrombin is a factor Va-dependent recognition site for the prothrombinase complex.Semantic proximity Read ↗

Heparin-activated antithrombin interacts with the autolysis loop of target coagulation proteases.Semantic proximity Read ↗

Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity.Semantic proximity Read ↗

Kinetic characterization of the proteinase binding defect in a reactive site variant of the serpin, antithrombin. Role of the P1' residue in transition-state stabilization of antithrombin-proteinase complex formation.Semantic proximity Read ↗

Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.Semantic proximity Read ↗

Substitution of arginine for Leu444 in the reactive site of heparin cofactor II enhances the rate of thrombin inhibition.Semantic proximity Read ↗

Contributions of basic amino acids in the autolysis loop of factor XIa to serpin specificity.Semantic proximity Read ↗

Contribution of amino acid region 334-335 from factor Va heavy chain to the catalytic efficiency of prothrombinase.Semantic proximity Read ↗

Heparin cofactor II is regulated allosterically and not primarily by template effects. Studies with mutant thrombins and glycosaminoglycans.Semantic proximity Read ↗

Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States.Semantic proximity Read ↗

Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins.Semantic proximity Read ↗

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