2rli
From Proteopedia
Solution structure of Cu(I) human Sco2
Structural highlights
DiseaseSCO2_HUMAN Defects in SCO2 are the cause of fatal infantile cardioencephalomyopathy with cytochrome c oxidase deficiency (FIC) [MIM:604377. This disease is characterized by hypertrophic cardiomyopathy, lactic acidosis, and gliosis. Heart and skeletal muscle show reductions in cytochrome c oxidase (COX) activity, whereas liver and fibroblasts show mild COX deficiencies.[1] [2] [3] FunctionSCO2_HUMAN Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHuman Sco2 is a mitochondrial membrane-bound protein involved in copper supply for the assembly of cytochrome c oxidase in eukaryotes. Its precise action is not yet understood. We report here a structural and dynamic characterization by NMR of the apo and copper(I) forms of the soluble fragment. The structural and metal binding features of human Cu(I)Sco2 are similar to the more often studied Sco1 homolog, although the dynamic properties and the conformational disorder are quite different when the apo forms and the copper(I)-loaded forms of the two proteins are compared separately. Such differences are accounted for in terms of the different physicochemical properties in strategic protein locations. The misfunction of the known pathogenic mutations is discussed on the basis of the obtained structure. A structural characterization of human SCO2.,Banci L, Bertini I, Ciofi-Baffoni S, Gerothanassis IP, Leontari I, Martinelli M, Wang S Structure. 2007 Sep;15(9):1132-40. PMID:17850752[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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