Sequence: RecName: Full=Nucleophosmin; Short=NPM; AltName: Full=Nucleolar phosphoprotein B23; AltName: Full=Nucleolar protein NO38; AltName: Full=Numatrin Description ..    ALK tyrosine kinase receptor Protein Family: Nucleoplasmin Comment ..    Confidence: Direct protein complex subunits assigned Gene Name: ALK Pref Name: NPM/ALK (Nucleophosmin/ALK tyrosine kinase receptor) Description: ALK tyrosine kinase receptor Synonyms: ALK tyrosine kinase receptor;Anaplastic lymphoma kinase;CD_antigen=CD246 Db Source: SWISS-PROT Db Version: 2012_01 ChEMBL target type: Target is a defined protein complex, consisting of multiple subunits Relationship Type: Direct protein target assigned Target Class L1: Enzyme Target Class L2: Kinase Target Class L3: Protein Kinase Target Class L4: Ser_Thr Target Class L5: Tkl Target Class L6: Stkr Target Class L7: Type1 Target Classification: enzyme kinase protein kinase ser_thr tkl stkr type1 Target Class L1: Nuclear other Target Classification: nuclear other Gene:NPM1     Related Protein 3D Structures

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Title: Structural insights into the ATP binding pocket of the anaplastic lymphoma kinase by site-directed mutagenesis, inhibitor binding analysis, and homology modeling.

Abstract: Anaplastic lymphoma kinase (ALK) is a valid target for anticancer therapy; however, potent ALK inhibitors suitable for clinical use are lacking. Because the majority of described kinase inhibitors bind in the ATP pocket of the kinase domain, we have characterized this pocket in ALK using site-directed mutagenesis, inhibition studies, and molecular modeling. Mutation of the gatekeeper residue, a key structural determinant influencing inhibitor binding, rendered the fusion protein, NPM/ALK, sensitive to inhibition by SKI-606 in the nanomolar range, while PD173955 inhibited the NPM/ALK mutant at micromolar concentrations. In contrast, both wild type and mutant NPM/ALK were insensitive to imatinib. Computer modeling indicated that docking solutions obtained with a homology model representing the intermediate conformation of the ALK kinase domain reflected closely experimental data. The good agreement between experimental and virtual results indicate that the ALK molecular models described here are useful tools for the rational design of ALK selective inhibitors. In addition, 4-phenylamino-quinoline compounds may have potential as templates for ALK inhibitors.
(PMID: 16970400)

Compounds with activity <= 50uM or explicitly reported as active by ChEMBL are flagged as active in this PubChem assay presentation.

ChEMBL Assay Type: Binding

ChEMBL Assay Data Source: Scientific Literature

ChEMBL Target ID: 105079

ChEMBL target type: Target is a defined protein complex, consisting of multiple subunits