2I5X

Engineering the PTPbeta catalytic domain with improved crystallization properties

Summary for 2I5X

• Entry DOI: 10.2210/pdb2i5x/pdb
• Related: 2I4G 2I4H
• Descriptor: Receptor-type tyrosine-protein phosphatase beta, CHLORIDE ION, (4-ETHYLPHENYL)SULFAMIC ACID, ... (5 entities in total)
• Functional Keywords: protein tyrosine phosphatase, wpd-loop, drug design, protein engineering, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein (Potential): P23467
• Total number of polymer chains: 2
• Total formula weight: 73073.77

Authors

Evdokimov, A.G.,Pokross, M.E.,Walter, R.L.,Mekel, M.,Klopfenstein, S. (deposition date: 2006-08-26, release date: 2006-09-05, Last modification date: 2023-08-30)

Primary citation

Evdokimov, A.G.,Pokross, M.,Walter, R.,Mekel, M.,Cox, B.,Li, C.,Bechard, R.,Genbauffe, F.,Andrews, R.,Diven, C.,Howard, B.,Rastogi, V.,Gray, J.,Maier, M.,Peters, K.G.
Engineering the catalytic domain of human protein tyrosine phosphatase beta for structure-based drug discovery.
Acta Crystallogr.,Sect.D, 62:1435-1445, 2006

PubMed 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.

PubMed: 17139078
DOI: 10.1107/S0907444906037784

Experimental method

X-RAY DIFFRACTION (1.7 Å)