4UXL

Structure of Human ROS1 Kinase Domain in Complex with PF-06463922


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.281 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.211 

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Ligand Structure Quality Assessment 


This is version 1.5 of the entry. See complete history


Literature

Pf-06463922 is a Potent and Selective Next-Generation Ros1/Alk Inhibitor Capable of Blocking Crizotinib-Resistant Ros1 Mutations.

Zou, H.Y.Li, Q.Engstrom, L.D.West, M.Appleman, V.Wong, K.A.Mctigue, M.Deng, Y.Liu, W.Brooun, A.Timofeevski, S.Mcdonnell, S.R.P.Jiang, P.Falk, M.D.Lappin, P.B.Affolter, T.Nichols, T.Hu, W.Lam, J.Johnson, T.W.Smeal, T.Charest, A.Fantin, V.R.

(2015) Proc Natl Acad Sci U S A 112: 3493

  • DOI: https://doi.org/10.1073/pnas.1420785112
  • Primary Citation of Related Structures:  
    4UXL

  • PubMed Abstract: 

    Oncogenic c-ros oncogene1 (ROS1) fusion kinases have been identified in a variety of human cancers and are attractive targets for cancer therapy. The MET/ALK/ROS1 inhibitor crizotinib (Xalkori, PF-02341066) has demonstrated promising clinical activity in ROS1 fusion-positive non-small cell lung cancer. However, emerging clinical evidence has shown that patients can develop resistance by acquiring secondary point mutations in ROS1 kinase. In this study we characterized the ROS1 activity of PF-06463922, a novel, orally available, CNS-penetrant, ATP-competitive small-molecule inhibitor of ALK/ROS1. In vitro, PF-06463922 exhibited subnanomolar cellular potency against oncogenic ROS1 fusions and inhibited the crizotinib-refractory ROS1(G2032R) mutation and the ROS1(G2026M) gatekeeper mutation. Compared with crizotinib and the second-generation ALK/ROS1 inhibitors ceritinib and alectinib, PF-06463922 showed significantly improved inhibitory activity against ROS1 kinase. A crystal structure of the PF-06463922-ROS1 kinase complex revealed favorable interactions contributing to the high-affinity binding. In vivo, PF-06463922 showed marked antitumor activity in tumor models expressing FIG-ROS1, CD74-ROS1, and the CD74-ROS1(G2032R) mutation. Furthermore, PF-06463922 demonstrated antitumor activity in a genetically engineered mouse model of FIG-ROS1 glioblastoma. Taken together, our results indicate that PF-06463922 has potential for treating ROS1 fusion-positive cancers, including those requiring agents with CNS-penetrating properties, as well as for overcoming crizotinib resistance driven by ROS1 mutation.


  • Organizational Affiliation

    Oncology Research Unit, helen.zou@pfizer.com.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ROS322Homo sapiensMutation(s): 0 
EC: 2.7.10.1
UniProt & NIH Common Fund Data Resources
Find proteins for P08922 (Homo sapiens)
Explore P08922 
Go to UniProtKB:  P08922
PHAROS:  P08922
GTEx:  ENSG00000047936 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08922
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
5P8
Query on 5P8

Download Ideal Coordinates CCD File 
B [auth A](10R)-7-amino-12-fluoro-2,10,16-trimethyl-15-oxo-10,15,16,17-tetrahydro-2H-8,4-(metheno)pyrazolo[4,3-h][2,5,11]benzoxadiazacyclotetradecine-3-carbonitrile
C21 H19 F N6 O2
IIXWYSCJSQVBQM-LLVKDONJSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
5P8 Binding MOAD:  4UXL Ki: 0.03 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.281 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.211 
  • Space Group: P 64
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 105.844α = 90
b = 105.844β = 90
c = 49.843γ = 120
Software Package:
Software NamePurpose
CNSrefinement
autoPROCdata reduction
SCALAdata scaling
CNXphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-03-11
    Type: Initial release
  • Version 1.1: 2015-03-18
    Changes: Database references
  • Version 1.2: 2015-04-15
    Changes: Database references
  • Version 1.3: 2019-04-24
    Changes: Data collection, Other, Source and taxonomy
  • Version 1.4: 2019-05-08
    Changes: Data collection, Experimental preparation
  • Version 1.5: 2024-01-10
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description