2rli

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(New page: 200px<br /> <applet load="2rli" size="450" color="white" frame="true" align="right" spinBox="true" caption="2rli" /> '''Solution structure of Cu(I) human Sco2'''<b...)
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[[Image:2rli.jpg|left|200px]]<br /><applet load="2rli" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2rli" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of Cu(I) human Sco2'''<br />
'''Solution structure of Cu(I) human Sco2'''<br />
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==Overview==
==Overview==
Human 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.
Human 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.
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==Disease==
 
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Known disease associated with this structure: Cardioencephalomyopathy, fatal infantile, due to cytochrome c oxidase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604272 604272]]
 
==About this Structure==
==About this Structure==
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2RLI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CU1 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2RLI OCA].
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2RLI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CU1:'>CU1</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLI OCA].
==Reference==
==Reference==
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[[Category: thioredoxin fold]]
[[Category: thioredoxin fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:37:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:58:42 2008''

Revision as of 10:58, 23 January 2008


2rli

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Solution structure of Cu(I) human Sco2

Overview

Human 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.

About this Structure

2RLI is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

A Structural Characterization of Human SCO2., Banci L, Bertini I, Ciofi-Baffoni S, Gerothanassis IP, Leontari I, Martinelli M, Wang S, Structure. 2007 Sep 11;15(9):1132-1140. PMID:17850752

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