2jo1: Difference between revisions
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'''Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles'''<br /> | '''Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2JO1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2JO1 is a [http://en.wikipedia.org/wiki/Single_protein 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=2JO1 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: na]] | [[Category: na]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:21:00 2008'' | ||
Revision as of 15:21, 23 January 2008
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Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles
OverviewOverview
FXYD1 is a major regulatory subunit of the Na,K-ATPase and the principal, substrate of hormone-regulated phosphorylation by c-AMP dependent protein, kinases A and C in heart and skeletal muscle sarcolemma. It is a member of, an evolutionarily conserved family of membrane proteins that regulate the, function of the enzyme complex in a tissue-specific and, physiological-state-specific manner. Here, we present the, three-dimensional structure of FXYD1 determined in micelles by NMR, spectroscopy. Structure determination was made possible by measuring, residual dipolar couplings in weakly oriented micelle samples of the, protein. This allowed us to obtain the relative orientations of the, helical segments and information about the protein dynamics. The, structural analysis was further facilitated by the inclusion of distance, restraints, obtained from paramagnetic spin label relaxation enhancements, and by refinement with a micelle depth restraint, derived from, paramagnetic Mn line broadening effects. The structure of FXYD1 provides, the foundation for understanding its intra-membrane association with the, Na,K-ATPase alpha subunit and suggests a mechanism whereby the, phosphorylation of conserved Ser residues, by protein kinases A and C, could induce a conformational change in the cytoplasmic domain of the, protein to modulate its interaction with the alpha subunit.
About this StructureAbout this Structure
2JO1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles., Teriete P, Franzin CM, Choi J, Marassi FM, Biochemistry. 2007 Jun 12;46(23):6774-83. Epub 2007 May 19. PMID:17511473
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