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

Citation:
Abstract
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)
1
Receptor-type Tyrosine-protein Phosphatase Beta(Gene symbol: PTPRB)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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