2jo1: Difference between revisions

Revision as of 11:25, 28 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:2jo1.png

Template:STRUCTURE 2jo1

Structure of the Na,K-ATPase regulatory protein FXYD1 in micellesStructure of the Na,K-ATPase regulatory protein FXYD1 in micelles

Template:ABSTRACT PUBMED 17511473

About this StructureAbout this Structure

2JO1 is a Single protein structure of sequence from Homo sapiens. Full experimental 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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OCA

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 {{STRUCTURE_2jo1|  PDB=2jo1  |  SCENE=  }}
-'''Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles'''
+===Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17511473}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17511473 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17511473}}
 ==About this Structure==
-JO1 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=2JO1 OCA].
+JO1 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=2JO1 OCA].
 ==Reference==
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 [[Category: Micelle]]
 [[Category: Na,k-atpase]]
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