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

Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin.

Biochemistry - 20 Apr 2021

Izaguirre Gonzalo, Swanson Richard, Roth Ryan, Gettins Peter G W, Olson Steven T

Abstract excerpt

Antithrombin is unique among serpin family protein protease inhibitors with respect to the major reactive center loop (RCL) and core conformational changes that mediate allosteric activation of its anticoagulant function by heparin. A critical role for expulsion of the RCL hinge from a native stabilizing interaction with the hydrophobic core in the activation mechanism has been proposed from reports that...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Antithrombins
Share to Disulfides

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

Share to Heparin

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 33822598
DOI: 10.1021/acs.biochem.1c00128
PMCID: PMC10921935

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

Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin.PMID 33822598Read ↗

Allosteric activation of antithrombin critically depends upon hinge region extension.Semantic proximity Read ↗

Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparin.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 ↗

Structure of prothrombin in the closed form reveals new details on the mechanism of activation.Semantic proximity Read ↗

Crystal structure of monomeric native antithrombin reveals a novel reactive center loop conformation.Semantic proximity Read ↗

Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Semantic proximity Read ↗

The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.Semantic proximity Read ↗

Cellular folding pathway of a metastable serpin.Semantic proximity Read ↗

Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa.Semantic proximity Read ↗

Expression and functional characterization of two natural heparin-binding site variants of antithrombin.Semantic proximity Read ↗

The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D.Semantic proximity Read ↗

Thrombosis as a conformational disease.Semantic proximity Read ↗

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