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

The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin.

The EMBO journal - 2 Jun 1997

van de Locht A, Bode W, Huber R, Le Bonniec B F, Stone S R, Esmon C T, Stubbs M T

Abstract excerpt

Previous crystal structures of thrombin indicate that the 60-insertion loop is a rigid moiety that partially occludes the active site, suggesting that this structural feature plays a decisive role in restricting thrombin's specificity. This restricted specificity is typified by the experimental observation that thrombin is not inhibited by micromolar concentrations of basic pancreatic trypsin inhibitor (BPTI)....

Read the complete abstract on PubMed

Topics

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

Share to Antithrombin III
Share to Hydrogen Bonding

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

Share to Models, Chemical

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Share to Thrombin

Source

Open in PubMed Open full text

Identifiers

PMID: 9214615
DOI: 10.1093/emboj/16.11.2977
PMCID: PMC1169916

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

The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin.PMID 9214615Read ↗

Thrombomodulin increases the rate of thrombin inhibition by BPTI.Semantic proximity Read ↗

Thrombomodulin changes the molecular surface of interaction and the rate of complex formation between thrombin and protein C.Semantic proximity Read ↗

The anticoagulant thrombin mutant W215A/E217A has a collapsed primary specificity pocket.Semantic proximity Read ↗

Mutation of W215 compromises thrombin cleavage of fibrinogen, but not of PAR1 or protein C.Semantic proximity Read ↗

Hirudin binding reveals key determinants of thrombin allostery.Semantic proximity Read ↗

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

How a Fragment Draws Attention to Selectivity Discriminating Features between the Related Proteases Trypsin and Thrombin.Semantic proximity Read ↗

X-ray structures of free and leupeptin-complexed human alphaI-tryptase mutants: indication for an alpha-->beta-tryptase transition.Semantic proximity Read ↗

A natural prothrombin mutant reveals an unexpected influence of A-chain structure on the activity of human alpha-thrombin.Semantic proximity Read ↗

Light Chain Mutation Effects on the Dynamics of Thrombin.Semantic proximity Read ↗

Dynamic Consequences of Mutation of Tryptophan 215 in Thrombin.Semantic proximity Read ↗

Elucidation of the molecular mechanisms of two nanobodies that inhibit thrombin-activatable fibrinolysis inhibitor activation and activated thrombin-activatable fibrinolysis inhibitor activity.Semantic proximity Read ↗

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