2ga7: Difference between revisions

Revision as of 16:18, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ga7.png

Template:STRUCTURE 2ga7

Solution structure of the copper(I) form of the third metal-binding domain of ATP7A protein (menkes disease protein)Solution structure of the copper(I) form of the third metal-binding domain of ATP7A protein (menkes disease protein)

Template:ABSTRACT PUBMED 16873374

About this StructureAbout this Structure

2GA7 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease protein., Banci L, Bertini I, Cantini F, DellaMalva N, Herrmann T, Rosato A, Wuthrich K, J Biol Chem. 2006 Sep 29;281(39):29141-7. Epub 2006 Jul 26. PMID:16873374

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Solution structure of the copper(I) form of the third metal-binding domain of ATP7A protein (menkes disease protein)'''
+===Solution structure of the copper(I) form of the third metal-binding domain of ATP7A protein (menkes disease protein)===
-==Overview==
+<!--
-The third metal-binding domain of the human Menkes protein (MNK3), a copper(I)-transporting ATPase, has been expressed in Escherichia coli and characterized in solution. The solution structure of MNK3, its copper(I)-binding properties, and its interaction with the physiological partner, HAH1, have been studied. MNK3 is the domain most dissimilar in structure from the other domains of the Menkes protein. This is reflected in a significant rearrangement of the last strand of the four-stranded beta-sheet when compared with the other known homologous proteins or protein domains. MNK3 is also peculiar with respect to its interaction with the copper(I) ion, as it was found to be a comparatively weak binder. Copper(I) transfer from metal-loaded HAH1 was observed experimentally, but the metal distribution was shifted toward binding by HAH1. This is at variance with what is observed for the other Menkes domains.
+The line below this paragraph, {{ABSTRACT_PUBMED_16873374}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16873374 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16873374}}
 ==About this Structure==
-GA7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GA7 OCA].
+GA7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GA7 OCA].
 ==Reference==
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 [[Category: Structural genomic]]
 [[Category: Structural proteomics in europe]]
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