3qcg | pdb_00003qcg

Human receptor protein tyrosine phosphatase gamma, domain 1, in complex with 3-[(3-bromo-4-chlorobenzyl)sulfanyl]thiophene-2-carboxylic acid

spinqualitylabelsall models 3qcg, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qcg is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACY, NX1 Related: 3qcb, 3qcc, 3qcd, 3qce, 3qcf, 3qch, 3qci, 3qcj, 3qck, 3qcl, 3qcm, 3qcn Gene: PTPG, PTPRG (HUMAN) Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PTPRG_HUMAN] Possesses tyrosine phosphatase activity. Publication Abstract from PubMed Protein tyrosine phosphatases (PTPs) catalyze the dephosphorylation of tyrosine residues, a process that involves a conserved tryptophan-proline-aspartate (WPD) loop in catalysis. In previously determined structures of PTPs, the WPD-loop has been observed in either an "open" conformation or a "closed" conformation. In the current work, X-ray structures of the catalytic domain of receptor-like protein tyrosine phosphatase gamma (RPTPgamma) revealed a ligand-induced "superopen" conformation not previously reported for PTPs. In the superopen conformation, the ligand acts as an apparent competitive inhibitor and binds in a small hydrophobic pocket adjacent to, but distinct from, the active site. In the open and closed WPD-loop conformations of RPTPgamma, the side chain of Trp1026 partially occupies this pocket. In the superopen conformation, Trp1026 is displaced allowing a 3,4-dichlorobenzyl substituent to occupy this site. The bound ligand prevents closure of the WPD-loop over the active site and disrupts the catalytic cycle of the enzyme. Small molecule receptor protein tyrosine phosphatase gamma (RPTPgamma) ligands that inhibit phosphatase activity via perturbation of the tryptophan-proline-aspartate (WPD) loop.,Sheriff S, Beno BR, Zhai W, Kostich WA, McDonnell PA, Kish K, Goldfarb V, Gao M, Kiefer SE, Yanchunas J, Huang Y, Shi S, Zhu S, Dzierba C, Bronson J, Macor JE, Appiah KK, Westphal RS, O'Connell J, Gerritz SW J Med Chem. 2011 Oct 13;54(19):6548-62. Epub 2011 Sep 20. PMID:21882820 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosine phosphatase

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