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

Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket.

The Journal of biological chemistry - 4 Mar 2005

Villa Fabrizio, Deak Maria, Bloomberg Graham B, Alessi Dario R, van Aalten Daan M F

Abstract excerpt

Protein-tyrosine phosphatase-L1 (PTPL1, also known as FAP-1, PTP1E, PTP-BAS, and PTPN13) is mutated in a significant number of colorectal tumors and may play a role in down-regulating signaling responses mediated by phosphatidylinositol 3-kinase, although the precise substrates are as yet unknown. In this study, we describe a 1.8 A resolution crystal structure of a fully active fragment of PTPL1 encompassing the...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Down-Regulation

Share to Phosphatidylinositol 3-Kinases

Share to Phosphotyrosine

Share to Protein Folding

Share to Protein Tyrosine Phosphatases

Share to Receptor, Insulin

Source

Identifiers

PMID: 15611135
DOI: 10.1074/jbc.M412211200

Genes

FAP
PTPN13

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket.PMID 15611135Read ↗

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

Crystal structure of a complex between protein tyrosine phosphatase 1B and the insulin receptor tyrosine kinase.Semantic proximity Read ↗

Biochemical, Enzymatic, and Computational Characterization of Recurrent Somatic Mutations of the Human Protein Tyrosine Phosphatase PTP1B in Primary Mediastinal B Cell Lymphoma.Semantic proximity Read ↗

Allele-specific inhibitors of protein tyrosine phosphatases.Semantic proximity Read ↗

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

Crystal structure of the human B-form low molecular weight phosphotyrosyl phosphatase at 1.6-A resolution.Semantic proximity Read ↗

Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B.Semantic proximity Read ↗

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

Structural analysis of the protein phosphatase 1 docking motif: molecular description of binding specificities identifies interacting proteins.Semantic proximity Read ↗

Use of Dominant-Negative/Substrate Trapping PTP Mutations to Search for PTP Interactors/Substrates.Semantic proximity Read ↗

Mutational analysis of the tyrosine phosphatome in colorectal cancers.Semantic proximity Read ↗

Crystal structure of the tyrosine kinase domain of the human insulin receptor.Semantic proximity Read ↗

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