1r7e: Difference between revisions
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'''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).''' | ||
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==About this Structure== | ==About this Structure== | ||
1R7E is a [[Single protein]] structure | 1R7E is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R7E OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Penin, F.]] | [[Category: Penin, F.]] | ||
[[Category: Ramboarina, S.]] | [[Category: Ramboarina, S.]] | ||
[[Category: | [[Category: Hcv ns5a protein]] | ||
[[Category: | [[Category: Membrane anchor domain]] | ||
[[Category: | [[Category: Nmr structure]] | ||
[[Category: | [[Category: Peptide.]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:10:39 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 07:10, 3 May 2008
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).
OverviewOverview
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.
About this StructureAbout this Structure
1R7E is a Single protein structure. Full crystallographic 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 Page seeded by OCA on Sat May 3 07:10:39 2008