2i3u
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span> |
|GENE= PTPRB, PTPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= PTPRB, PTPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2hc1|2HC1]], [[2hc2|2HC2]], [[2i3r|2I3R]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3u OCA], [http://www.ebi.ac.uk/pdbsum/2i3u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i3u RCSB]</span> | ||
}} | }} | ||
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[[Category: wpd-loop]] | [[Category: wpd-loop]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:39:17 2008'' |
Revision as of 00:39, 31 March 2008
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| , resolution 1.850Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | PTPRB, PTPB (Homo sapiens) | ||||||
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
| Related: | 2HC1, 2HC2, 2I3R
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors
Overview
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.
About this Structure
2I3U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Engineering the catalytic domain of human protein tyrosine phosphatase beta for structure-based drug discovery., Evdokimov AG, 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 KG, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1435-45. Epub 2006, Nov 23. PMID:17139078
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