1r7e: Difference between revisions

Revision as of 15:37, 27 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:1r7e.png

Template:STRUCTURE 1r7e

NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure. Sample in 100mM SDS).NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure. Sample in 100mM SDS).

Template:ABSTRACT PUBMED 15247283

About this StructureAbout this Structure

1R7E is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A., Penin F, Brass V, Appel N, Ramboarina S, Montserret R, Ficheux D, Blum HE, Bartenschlager R, Moradpour D, J Biol Chem. 2004 Sep 24;279(39):40835-43. Epub 2004 Jul 7. PMID:15247283

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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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-[[Image:1r7e.jpg|left|200px]]
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 {{STRUCTURE_1r7e|  PDB=1r7e  |  SCENE=  }}
-'''NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure. Sample in 100mM SDS).'''
+===NMR structure of the membrane anchor domain (1-31) of the nonstructural protein 5A (NS5A) of hepatitis C virus (Minimized average structure. Sample in 100mM SDS).===
-==Overview==
+<!--
-Hepatitis C virus (HCV) nonstructural protein 5A (NS5A) is a membrane-associated, essential component of the viral replication complex. Here, we report the three-dimensional structure of the membrane anchor domain of NS5A as determined by NMR spectroscopy. An alpha-helix extending from amino acid residue 5 to 25 was observed in the presence of different membrane mimetic media. This helix exhibited a hydrophobic, Trprich side embedded in detergent micelles, while the polar, charged side was exposed to the solvent. Thus, the NS5A membrane anchor domain forms an in-plane amphipathic alpha-helix embedded in the cytosolic leaflet of the membrane bilayer. Interestingly, mutations affecting the positioning of fully conserved residues located at the cytosolic surface of the helix impaired HCV RNA replication without interfering with the membrane association of NS5A. In conclusion, the NS5A membrane anchor domain constitutes a unique platform that is likely involved in specific interactions essential for the assembly of the HCV replication complex and that may represent a novel target for antiviral intervention.
+The line below this paragraph, {{ABSTRACT_PUBMED_15247283}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15247283 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15247283}}
 ==About this Structure==
-R7E is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R7E OCA].
+R7E is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R7E OCA].
 ==Reference==
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 [[Category: Nmr structure]]
 [[Category: Peptide.]]
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