2I4E: Structural Studies Of Protein Tyrosine Phosphatase Beta Catalytic Domain In Complex With Inhibitors

Protein tyrosine phosphatases (PTPs) play roles in many biological processes and are considered to be important targets for drug discovery. As inhibitor development has proven challenging, crystal structure-based design will be very helpful to advance inhibitor potency and selectivity. Successful application of protein crystallography to drug discovery heavily relies on high-quality crystal structures of the protein of interest complexed with pharmaceutically interesting ligands. It is very important to be able to produce protein-ligand crystals rapidly and reproducibly for as many ligands as necessary. This study details our efforts to engineer the catalytic domain of human protein tyrosine phosphatase beta (HPTPbeta-CD) with properties suitable for rapid-turnaround crystallography. Structures of apo HPTPbeta-CD and its complexes with several novel small-molecule inhibitors are presented here for the first time.
PDB ID: 2I4EDownload
MMDB ID: 41209
PDB Deposition Date: 2006/8/21
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 1.75  Å
Source Organism:
Similar Structures:
Biological Unit for 2I4E: monomeric; determined by author
Molecular Components in 2I4E
Label Count Molecule
Protein (1 molecule)
Receptor-type Tyrosine-protein Phosphatase Beta(Gene symbol: PTPRB)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB