Tetrathiomolybdate inhibits copper trafficking proteins through metal cluster formation

Science

Volumn 327, Issue 5963, 2010, Pages 331-334

  Alvarez, Hamsell M ^a   Xue, Yi ^a   Robinson, Chandler D ^a   Canalizo Hernández, Mónica A ^a   Marvin, Rebecca G ^a   Kelly, Rebekah A ^b   Mondragón, Alfonso ^a   Penner Hahn, James E ^b   O'Halloran, Thomas V ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATX1 PROTEIN; CHAPERONE; COPPER; IRON SULFUR PROTEIN; METAL COMPLEX; MOLYBDENUM; SULFUR; TETRATHIOMOLYBDIC ACID; UNCLASSIFIED DRUG;

AMMONIUM COMPOUND; ANIMAL; COPPER; CRYSTALLOGRAPHY; DISEASE TREATMENT; DRUG; ENZYME ACTIVITY; INHIBITION; KETONE; MOLYBDENUM; PROTEIN; SPECTROSCOPY;

ARTICLE; COMPLEX FORMATION; COPPER METABOLISM; CRYSTALLOGRAPHY; DOWN REGULATION; DRUG MECHANISM; DRUG PROTEIN BINDING; ENZYME RELEASE; METAL METABOLISM; PRIORITY JOURNAL; SPECTROSCOPY; WILSON DISEASE;

CARRIER PROTEINS; CATION TRANSPORT PROTEINS; COPPER; CRYSTALLOGRAPHY, X-RAY; LIGANDS; METALLOCHAPERONES; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MOLYBDENUM; OXIDATION-REDUCTION; PHYSICOCHEMICAL PROCESSES; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE PROTEINS;

ANIMALIA;

EID: 74549178479     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1179907     Document Type: Article

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33. This manuscript is dedicated to the memory of E. Stiefel and his contributions to the field of molybdenum sulfide chemistry. This work was supported by grant GM54222 and GM38784 (T.V.O.) and GM38047 (J.E.P.-H.) from the NIH. The Robert H. Lurie Comprehensive Cancer Center provided a Malkin Fellowship (H.M.A.) and support for Structural Biology Facility. Use of the Advanced Photon Source [Structural Biology Center-Collaborative Access Team (CAT) and Industrial Macromolecular Crystallography Association CAT] and the Stanford Synchrotron Radiation Laboratory (SSRL) was supported by the U.S. Department of Energy, Office of Basic Energy Sciences, with additional support (at SSRL) from the National Center for Research Resources, NIH. Use of the Chicago Biomedical Consortium (CBO-University of Illinois at Chicago Proteomics Facility was supported by The Searle Funds at the CBC, and use of LA-ICP-MS was supported by a National Aeronautics and Space Administration grant to the Quantitative Bioelement Imaging Center in the Chemistry of Life Processes Institute at Northwestern University. We thank P. Focia for assistance with x-ray diffraction collection, M. Clausén for assistance in the early stages of XAS measurements, Y. Wang for assistance with the protein MS, A. Davis for providing opo-Ccc2a, and A. Mazar for helpful discussions. The atomic coordinates have been deposited at the Protein Data Bank with code 3K7R.