6BO7

Crystal structure of Plasmodium vivax hypoxanthine guanine phosphoribosyltransferase in complex with [3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.86 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.231 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

Design of Plasmodium vivax Hypoxanthine-Guanine Phosphoribosyltransferase Inhibitors as Potential Antimalarial Therapeutics.

Keough, D.T.Rejman, D.Pohl, R.Zbornikova, E.Hockova, D.Croll, T.Edstein, M.D.Birrell, G.W.Chavchich, M.Naesens, L.M.J.Pierens, G.K.Brereton, I.M.Guddat, L.W.

(2018) ACS Chem Biol 13: 82-90

  • DOI: https://doi.org/10.1021/acschembio.7b00916
  • Primary Citation of Related Structures:  
    5HIA, 6BNJ, 6BO7

  • PubMed Abstract: 

    Plasmodium falciparum (Pf) and Plasmodium vivax (Pv) are the foremost causative agents of malaria. Due to the development of resistance to current antimalarial medications, new drugs for this parasitic disease need to be discovered. The activity of hypoxanthine-guanine-[xanthine]-phosphoribosyltransferase, HG[X]PRT, is reported to be essential for the growth of both of these parasites, making it an excellent target for antimalarial drug discovery. Here, we have used rational structure-based methods to design an inhibitor, [3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine, of PvHGPRT and PfHGXPRT that has K i values of 8 and 7 nM, respectively, for these two enzymes. The crystal structure of PvHGPRT in complex with this compound has been determined to 2.85 Å resolution. The corresponding complex with human HGPRT was also obtained to allow a direct comparison of the binding modes of this compound with the two enzymes. The tetra-(ethyl l-phenylalanine) tetraamide prodrug of this compound was synthesized, and it has an IC 50 of 11.7 ± 3.2 μM against Pf lines grown in culture and a CC 50 in human A549 cell lines of 102 ± 11 μM, thus giving it a ∼10-fold selectivity index.


  • Organizational Affiliation

    School of Chemistry and Molecular Biosciences, The University of Queensland , Brisbane 4072, Australia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hypoxanthine phosphoribosyltransferase
A, B, C, D, E
A, B, C, D, E, F, G, H, I, J, K, L
238Plasmodium vivaxMutation(s): 0 
Gene Names: PVC01_080017300PVP01_0812500PVT01_080017400
EC: 2.4.2.8
UniProt
Find proteins for A5K7E9 (Plasmodium vivax (strain Salvador I))
Explore A5K7E9 
Go to UniProtKB:  A5K7E9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA5K7E9
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
YPG
Query on YPG

Download Ideal Coordinates CCD File 
BA [auth E]
EA [auth F]
HA [auth G]
KA [auth H]
NA [auth I]
BA [auth E],
EA [auth F],
HA [auth G],
KA [auth H],
NA [auth I],
O [auth A],
QA [auth J],
R [auth B],
U [auth C],
UA [auth K],
X [auth D],
YA [auth L]
[3-[(3~{R},4~{R})-3-(2-azanyl-6-oxidanylidene-1~{H}-purin-9-yl)-4-[(2~{S})-2-oxidanyl-2-phosphono-ethoxy]pyrrolidin-1-y l]-3-oxidanylidene-propyl]phosphonic acid
C14 H22 N6 O10 P2
RBYFDIJTTUISNF-MRTMQBJTSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
AA [auth E]
CA [auth F]
DA [auth F]
FA [auth G]
GA [auth G]
AA [auth E],
CA [auth F],
DA [auth F],
FA [auth G],
GA [auth G],
IA [auth H],
JA [auth H],
LA [auth I],
M [auth A],
MA [auth I],
N [auth A],
OA [auth J],
P [auth B],
PA [auth J],
Q [auth B],
RA [auth K],
S [auth C],
SA [auth K],
T [auth C],
TA [auth K],
V [auth D],
VA [auth L],
W [auth D],
WA [auth L],
XA [auth L],
Y [auth E],
Z [auth E]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.86 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.231 
  • Space Group: P 2 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 55.784α = 90
b = 219.854β = 90
c = 254.139γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Health and Medical Research Council (NHMRC, Australia)Australia1030353

Revision History  (Full details and data files)

  • Version 1.0: 2017-12-13
    Type: Initial release
  • Version 1.1: 2018-01-31
    Changes: Database references
  • Version 1.2: 2020-01-08
    Changes: Author supporting evidence
  • Version 1.3: 2024-03-13
    Changes: Data collection, Database references, Derived calculations, Structure summary