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3QCN

Human receptor protein tyrosine phosphatase gamma, domain 1, trigonal crystal form

Summary for 3QCN
Entry DOI10.2210/pdb3qcn/pdb
Related3QCB 3QCC 3QCD 3QCE 3QCF 3QCG 3QCH 3QCI 3QCJ 3QCK 3QCL 3QCM
DescriptorReceptor-type tyrosine-protein phosphatase gamma (2 entities in total)
Functional Keywordstyrosine receptor phosphatase, twisted mixed beta-sheets flanked by {alpha}-helices, hydrolase, apo
Biological sourceHomo sapiens (human)
Cellular locationMembrane; Single-pass type I membrane protein (Probable): P23470
Total number of polymer chains1
Total formula weight35705.53
Authors
Sheriff, S. (deposition date: 2011-01-16, release date: 2011-12-28, Last modification date: 2023-09-13)
Primary citationSheriff, S.,Beno, B.R.,Zhai, W.,Kostich, W.A.,McDonnell, P.A.,Kish, K.,Goldfarb, V.,Gao, M.,Kiefer, S.E.,Yanchunas, J.,Huang, Y.,Shi, S.,Zhu, S.,Dzierba, C.,Bronson, J.,Macor, J.E.,Appiah, K.K.,Westphal, R.S.,O'Connell, J.,Gerritz, S.W.
Small molecule receptor protein tyrosine phosphatase [gamma](RPTP[gamma]) ligands that inhibit phosphatase activity via perturbation of the tryptophan-proline-aspartate (WPD) loop
J.Med.Chem., 54:6548-6562, 2011
Cited by
PubMed Abstract: 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 γ (RPTPγ) 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 RPTPγ, 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.
PubMed: 21882820
DOI: 10.1021/jm2003766
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.41 Å)
Structure validation

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