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

Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition.

1 Nov 1994

Abstract excerpt

One feature that distinguishes all of the inhibitory members of the serpin gene family is the presence of a small uncharged residue at the P14 position of the reactive center loop. In this report we examine the effects of mutations at this position, in the serpin, plasminogen activator inhibitor type 1 (PAI-1). Replacement of the native P14 Thr-333 residue by an Arg (Thr-333-->Arg) resulted in complete loss of...

Read the complete abstract on PubMed

Topics

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

Share to Blood Coagulation and Thrombosis Mechanisms
Share to Protease and Inhibitor Mechanisms
Share to Signaling Pathways in Disease

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

Source

Identifiers

PMID: 7961684
DOI: 10.1016/s0021-9258(18)47036-6

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

Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition.PMID 7961684Read ↗

Plasminogen activator inhibitor-2 is highly tolerant to P8 residue substitution--implications for serpin mechanistic model and prediction of nsSNP activities.Semantic proximity Read ↗

The M358R variant of α(1)-proteinase inhibitor inhibits coagulation factor VIIa.Semantic proximity Read ↗

Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide.Semantic proximity Read ↗

Structural basis for serpin inhibitor activity.Semantic proximity Read ↗

The role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsin.Semantic proximity Read ↗

Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation.Semantic proximity Read ↗

The story of the serpin plasminogen activator inhibitor 1: is there any need for another mutant?Semantic proximity Read ↗

The Molecular Basis for Anti-Proteolytic and Non-Proteolytic Functions of Plasminogen Activator Inhibitor Type-1: Roles of the Reactive Centre Loop, the Shutter Region, the Flexible Joint Region and the Small Serpin FragmentSemantic proximity Read ↗

Substrate behavior of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop.Semantic proximity Read ↗

The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion.Semantic proximity Read ↗

An overview of the serpin superfamily.Semantic proximity Read ↗

Interaction between the P14 residue and strand 2 of beta-sheet B is critical for reactive center loop insertion in plasminogen activator inhibitor-2.Semantic proximity Read ↗

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