5T4B: Human Dpp4 In Complex With A Ligand 34a

Citation:
Abstract
Molecular modeling of unbound tricyclic guanine scaffolds indicated that they can serve as effective bioisosteric replacements of xanthines. This notion was further confirmed by a combination of X-ray crystallography and SAR studies, indicating that tricyclic guanine DPP4 inhibitors mimic the binding mode of xanthine inhibitors, exemplified by linagliptin. Realization of the bioisosteric relationship between these scaffolds potentially will lead to a wider application of cyclic guanines as xanthine replacements in drug discovery programs for a variety of biological targets. Newly designed DPP4 inhibitors achieved sub-nanomolar potency range and demonstrated oral activity in vivo in mouse glucose tolerance test.
PDB ID: 5T4BDownload
MMDB ID: 143867
PDB Deposition Date: 2016/8/29
Updated in MMDB: 2016/10
Experimental Method:
x-ray diffraction
Resolution: 1.76  Å
Source Organism:
Similar Structures:
Biological Unit for 5T4B: dimeric; determined by author and by software (PISA)
Molecular Components in 5T4B
Label Count Molecule
Proteins (2 molecules)
2
Dipeptidyl Peptidase 4(Gene symbol: DPP4)
Molecule annotation
Chemicals (22 molecules)
1
19
2
2
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.