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

Structural analysis of protein tyrosine phosphatase 1B reveals potentially druggable allosteric binding sites.

Proteins - 1 Mar 2018

Kumar Ammu Prasanna, Nguyen Minh N, Verma Chandra, Lukman Suryani

Abstract excerpt

Catalytic proteins such as human protein tyrosine phosphatase 1B (PTP1B), with conserved and highly polar active sites, warrant the discovery of druggable nonactive sites, such as allosteric sites, and potentially, therapeutic small molecules that can bind to these sites. Catalyzing the dephosphorylation of numerous substrates, PTP1B is physiologically important in intracellular signal transduction pathways in...

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 Allosteric Site
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Inhibitors

Share to Ligands

Share to Principal Component Analysis

Share to Protein Conformation

Share to Protein Tyrosine Phosphatase, Non-Receptor Type 1

Source

Identifiers

PMID: 29235148
DOI: 10.1002/prot.25440

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural analysis of protein tyrosine phosphatase 1B reveals potentially druggable allosteric binding sites.PMID 29235148Read ↗

Structures of human PTP1B variants reveal allosteric sites to target for weight loss therapySemantic proximity Read ↗

Evolutionarily Conserved Allosteric Communication in Protein Tyrosine PhosphatasesSemantic proximity Read ↗

The mechanism of allosteric inhibition of protein tyrosine phosphatase 1B.Semantic proximity Read ↗

Distal Mutations Rewire Allosteric Networks to Control Substrate Specificity in PTP1B.Semantic proximity Read ↗

Structure-based design of selective and potent inhibitors of protein-tyrosine phosphatase beta.Semantic proximity Read ↗

High-resolution double vision of the archetypal protein tyrosine phosphataseSemantic proximity Read ↗

Discovery of a novel series of inhibitors of lymphoid tyrosine phosphatase with activity in human T cells.Semantic proximity Read ↗

Detecting similar binding pockets to enable systems polypharmacologySemantic proximity Read ↗

Protein Tyrosine Phosphatase 1B (PTP1B): Insights into its New Implications in TumorigenesisSemantic proximity Read ↗

Insights into the key interactions between human protein phosphatase 5 and cantharidin using molecular dynamics and site-directed mutagenesis bioassays.Semantic proximity Read ↗

Conformation-assisted inhibition of protein-tyrosine phosphatase-1B elicits inhibitor selectivity over T-cell protein-tyrosine phosphatase.Semantic proximity Read ↗

Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.Semantic proximity Read ↗

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