2OAE

Crystal structure of rat dipeptidyl peptidase (DPPIV) with thiazole-based peptide mimetic #31


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.249 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Pyrrolidine-constrained phenethylamines: The design of potent, selective, and pharmacologically efficacious dipeptidyl peptidase IV (DPP4) inhibitors from a lead-like screening hit.

Backes, B.J.Longenecker, K.Hamilton, G.L.Stewart, K.Lai, C.Kopecka, H.von Geldern, T.W.Madar, D.J.Pei, Z.Lubben, T.H.Zinker, B.A.Tian, Z.Ballaron, S.J.Stashko, M.A.Mika, A.K.Beno, D.W.Kempf-Grote, A.J.Black-Schaefer, C.Sham, H.L.Trevillyan, J.M.

(2007) Bioorg Med Chem Lett 17: 2005-2012

  • DOI: https://doi.org/10.1016/j.bmcl.2007.01.026
  • Primary Citation of Related Structures:  
    2OAE, 2OAG

  • PubMed Abstract: 

    A novel series of pyrrolidine-constrained phenethylamines were developed as dipeptidyl peptidase IV (DPP4) inhibitors for the treatment of type 2 diabetes. The cyclohexene ring of lead-like screening hit 5 was replaced with a pyrrolidine to enable parallel chemistry, and protein co-crystal structural data guided the optimization of N-substituents. Employing this strategy, a >400x improvement in potency over the initial hit was realized in rapid fashion. Optimized compounds are potent and selective inhibitors with excellent pharmacokinetic profiles. Compound 30 was efficacious in vivo, lowering blood glucose in ZDF rats that were allowed to feed freely on a mixed meal.


  • Organizational Affiliation

    Metabolic Disease Research, Abbott Laboratories, Abbott Park Road, Abbott Park, IL 60064-6099, USA. bradley.backes@abbott.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Dipeptidyl peptidase 4
A, B
730Rattus norvegicusMutation(s): 0 
EC: 3.4.14.5
UniProt
Find proteins for P14740 (Rattus norvegicus)
Explore P14740 
Go to UniProtKB:  P14740
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP14740
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
AIL
Query on AIL

Download Ideal Coordinates CCD File 
D [auth A]N-{[(3S,5S)-5-(1,3-THIAZOLIDIN-3-YLCARBONYL)PYRROLIDIN-3-YL]METHYL}-1,3-THIAZOLE-4-CARBOXAMIDE
C13 H18 N4 O2 S2
KFQMVMSMRNCTET-UWVGGRQHSA-N
SO4
Query on SO4

Download Ideal Coordinates CCD File 
C [auth A]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Binding Affinity Annotations 
IDSourceBinding Affinity
AIL BindingDB:  2OAE Ki: 3.4 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.249 
  • Space Group: P 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 208.349α = 90
b = 208.349β = 90
c = 208.349γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
PDB_EXTRACTdata extraction
HKL-2000data collection

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-02-27
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description
  • Version 1.4: 2023-12-27
    Changes: Data collection, Database references, Derived calculations