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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.1 Classification:SUGAR BINDING PROTEIN Release Date:2018-02-28 Deposition Date:2017-08-23 Revision Date: Molecular Weight:36674.99 Macromolecule Type:Protein Residue Count:332 Atom Site Count:2382 DOI:10.2210/pdb6as8/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.55 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-08-17 Revision Date: Molecular Weight:40486.95 Macromolecule Type:Protein Residue Count:328 Atom Site Count:2902 DOI:10.2210/pdb5os8/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.78 Classification:OXYGEN TRANSPORT Release Date:2018-02-28 Deposition Date:2017-02-14 Revision Date: Molecular Weight:18583.05 Macromolecule Type:Protein Residue Count:154 Atom Site Count:1291 DOI:10.2210/pdb5ut8/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.81 Classification:HYDROLASE Release Date:2018-02-28 Deposition Date:2017-06-22 Revision Date: Molecular Weight:50311.3 Macromolecule Type:Protein Residue Count:432 Atom Site Count:3307 DOI:10.2210/pdb5xu8/pdb Abstract: Ubiquitin-specific protease 2 (USP2) belongs to the family of deubiquitinases that can rescue protein targets from proteasomal degradation by reversing their ubiquitination. In various cancers, including prostate cancer and ovarian carcinoma, upregulation of USP2 leads to an increase in the levels of deubiquitinated substrates such as fatty acid synthase, MDM2, cyclin D1 and Aurora-A. USP2 thus plays a critical role in tumor cells' survival and therefore represents a therapeutic target. Here a leukemia drug, 6-thioguanine, was found to be a potent inhibitor of USP2. Enzyme-kinetic and X-ray crystallographic data suggest that 6-thioguanine displays a noncompetitive and slow-binding inhibitory mechanism against USP2. Our study provides a clear rationale for the clinical evaluation of 6-thioguanine for USP2-upregulated cancers.
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.89 Classification:TOXIN Release Date:2018-02-28 Deposition Date:2017-09-01 Revision Date: Molecular Weight:3877.48 Macromolecule Type:Protein Residue Count:35 Atom Site Count:228 DOI:10.2210/pdb6av8/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.85 Classification:CELL ADHESION Release Date:2018-02-28 Deposition Date:2017-02-25 Revision Date: Molecular Weight:37227.53 Macromolecule Type:Protein Residue Count:334 Atom Site Count:2557 DOI:10.2210/pdb5uz8/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.62 Classification:HYDROLASE Release Date:2018-02-28 Deposition Date:2017-02-05 Revision Date: Molecular Weight:34523.43 Macromolecule Type:Protein Residue Count:306 Atom Site Count:2437 DOI:10.2210/pdb5n19/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.6 Classification:MEMBRANE PROTEIN Release Date:2018-02-28 Deposition Date:2017-11-23 Revision Date: Molecular Weight:29534.27 Macromolecule Type:Protein Residue Count:258 Atom Site Count:2041 DOI:10.2210/pdb6f29/pdb Abstract: Starting from 1-4 and 7 structural templates, analogues based on bioisosteric replacements (5a-c vs 1, 2 and 6 vs 7) were synthesized for completing the SAR analysis. Interesting binding properties at GluA2, GluK1, and GluK3 receptors were discovered. The requirements for GluK3 interaction were elucidated by determining the X-ray structures of the GluK3-LBD with 2 and 5c and by computational studies. Antinociceptive potential was demonstrated for GluK1 partial agonist 3 and antagonist 7 (2 mg/kg ip).
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.45 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-02-08 Revision Date: Molecular Weight:43785.94 Macromolecule Type:Protein Residue Count:372 Atom Site Count:3009 DOI:10.2210/pdb5n39/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:NEUTRON DIFFRACTION, X-RAY DIFFRACTION Resolution: Classification:lyase/lyase inhibitor Release Date:2018-02-28 Deposition Date:2017-10-20 Revision Date: Molecular Weight:29678.91 Macromolecule Type:Protein Residue Count:260 Atom Site Count:2069 DOI:10.2210/pdb6bc9/pdb Abstract: Human carbonic anhydrases (hCAs) play various roles in cells, and have been drug targets for decades. Sequence similarities of hCA isoforms necessitate designing specific inhibitors, which requires detailed structural information for hCA-inhibitor complexes. We present room temperature neutron structures of hCA II in complex with three clinical drugs that provide in-depth analysis of drug binding, including protonation states of the inhibitors, hydration water structure, and direct visualization of hydrogen-bonding networks in the enzyme's active site. All sulfonamide inhibitors studied bind to the Zn metal center in the deprotonated, anionic, form. Other chemical groups of the drugs can remain neutral or be protonated when bound to hCA II. MD simulations have shown that flexible functional groups of the inhibitors may alter their conformations at room temperature and occupy different sub-sites. This study offers insights into the design of specific drugs to target cancer-related hCA isoform IX.
Data Types:
  • Tabular Data
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