4JBP

Novel Aurora kinase inhibitors reveal mechanisms of HURP in nucleation of centrosomal and kinetochore microtubules


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.223 
  • R-Value Observed: 0.226 

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Ligand Structure Quality Assessment 


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Literature

Aurora kinase inhibitors reveal mechanisms of HURP in nucleation of centrosomal and kinetochore microtubules.

Wu, J.M.Chen, C.T.Coumar, M.S.Lin, W.H.Chen, Z.J.Hsu, J.T.Peng, Y.H.Shiao, H.Y.Lin, W.H.Chu, C.Y.Wu, J.S.Lin, C.T.Chen, C.P.Hsueh, C.C.Chang, K.Y.Kao, L.P.Huang, C.Y.Chao, Y.S.Wu, S.Y.Hsieh, H.P.Chi, Y.H.

(2013) Proc Natl Acad Sci U S A 110: E1779-E1787

  • DOI: https://doi.org/10.1073/pnas.1220523110
  • Primary Citation of Related Structures:  
    4JBO, 4JBP, 4JBQ

  • PubMed Abstract: 

    The overexpression of Aurora kinases in multiple tumors makes these kinases appealing targets for the development of anticancer therapies. This study identified two small molecules with a furanopyrimidine core, IBPR001 and IBPR002, that target Aurora kinases and induce a DFG conformation change at the ATP site of Aurora A. Our results demonstrate the high potency of the IBPR compounds in reducing tumorigenesis in a colorectal cancer xenograft model in athymic nude mice. Human hepatoma up-regulated protein (HURP) is a substrate of Aurora kinase A, which plays a crucial role in the stabilization of kinetochore fibers. This study used the IBPR compounds as well as MLN8237, a proven Aurora A inhibitor, as chemical probes to investigate the molecular role of HURP in mitotic spindle formation. These compounds effectively eliminated HURP phosphorylation, thereby revealing the coexistence and continuous cycling of HURP between unphosphorylated and phosphorylated forms that are associated, respectively, with microtubules emanating from centrosomes and kinetochores. Furthermore, these compounds demonstrate a spatial hierarchical preference for HURP in the attachment of microtubules extending from the mother to the daughter centrosome. The finding of inequality in the centrosomal microtubules revealed by these small molecules provides a versatile tool for the discovery of new cell-division molecules for the development of antitumor drugs.


  • Organizational Affiliation

    Institutes of Biotechnology and Pharmaceutical Research, National Health Research Institutes, Zhunan 35053, Taiwan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Aurora Kinase A279Homo sapiensMutation(s): 1 
Gene Names: AURKAAIKAIRK1ARK1AURAAYK1BTAKIAK1STK15STK6
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for O14965 (Homo sapiens)
Explore O14965 
Go to UniProtKB:  O14965
PHAROS:  O14965
GTEx:  ENSG00000087586 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO14965
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
YPH
Query on YPH

Download Ideal Coordinates CCD File 
B [auth A]1-(4-{2-[(6-{4-[2-(4-hydroxypiperidin-1-yl)ethoxy]phenyl}furo[2,3-d]pyrimidin-4-yl)amino]ethyl}phenyl)-3-phenylurea
C34 H36 N6 O4
WEVRAOPLGYJTLY-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
YPH Binding MOAD:  4JBP IC50: 41 (nM) from 1 assay(s)
BindingDB:  4JBP IC50: 41 (nM) from 1 assay(s)
PDBBind:  4JBP IC50: 41 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.291 
  • R-Value Work: 0.223 
  • R-Value Observed: 0.226 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 80.81α = 90
b = 80.81β = 90
c = 174.308γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACTdata extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-06-05
    Type: Initial release
  • Version 1.1: 2024-03-20
    Changes: Data collection, Database references, Derived calculations