2ajm: Difference between revisions

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[[Image:2ajm.gif|left|200px]]
{{Seed}}
[[Image:2ajm.png|left|200px]]


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{{STRUCTURE_2ajm|  PDB=2ajm  |  SCENE=  }}  
{{STRUCTURE_2ajm|  PDB=2ajm  |  SCENE=  }}  


'''NMR structure of the in-plane membrane anchor domain [1-28] of the monotopic NonStructural Protein 5A (NS5A) from the Bovine Viral Diarrhea Virus (BVDV)'''
===NMR structure of the in-plane membrane anchor domain [1-28] of the monotopic NonStructural Protein 5A (NS5A) from the Bovine Viral Diarrhea Virus (BVDV)===




==Overview==
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Hepatitis C virus (HCV) nonstructural protein 5A (NS5A) is a monotopic membrane protein anchored to the membrane by an N-terminal in-plane amphipathic alpha-helix. This membrane anchor is essential for the assembly of a functional viral replication complex. Although amino acid sequences differ considerably, putative membrane anchors with amphipathic features were predicted in NS5A from related Flaviviridae family members, in particular bovine viral diarrhea virus (BVDV), the prototype representative of the genus Pestivirus. We report here the NMR structure of the membrane anchor 1-28 of NS5A from BVDV in the presence of different membrane mimetic media. This anchor includes a long amphipathic alpha-helix of 21 residues interacting in-plane with the membrane interface and including a putative flexible region. Molecular dynamic simulation at a water-dodecane interface used to mimic the surface separating a lipid bilayer and an aqueous medium demonstrated the stability of the helix orientation and the location at the hydrophobic-hydrophilic interface. The flexible region of the helix appears to be required to allow the most favorable interaction of hydrophobic and hydrophilic side chain residues with their respective environment at the membrane interface. Despite the lack of amino acid sequence similarity, this amphipathic helix shares common structural features with that of the HCV counterpart, including a stable, hydrophobic N-terminal segment separated from the more hydrophilic C-terminal segment by a local, flexible region. These structural conservations point toward conserved roles of the N-terminal in-plane membrane anchors of NS5A in replication complex formation of HCV, BVDV, and other related viruses.
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{{ABSTRACT_PUBMED_16475810}}


==About this Structure==
==About this Structure==
2AJM is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJM OCA].  
2AJM is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AJM OCA].  


==Reference==
==Reference==
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[[Category: Amphipathic alpha-helix]]
[[Category: Amphipathic alpha-helix]]
[[Category: In-plane membrane anchor domain]]
[[Category: In-plane membrane anchor domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:07:57 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:31:55 2008''

Revision as of 12:32, 28 July 2008

File:2ajm.png

Template:STRUCTURE 2ajm

NMR structure of the in-plane membrane anchor domain [1-28] of the monotopic NonStructural Protein 5A (NS5A) from the Bovine Viral Diarrhea Virus (BVDV)

Template:ABSTRACT PUBMED 16475810

About this Structure

2AJM is a Single protein structure. Full experimental information is available from OCA.

Reference

NMR structure and molecular dynamics of the in-plane membrane anchor of nonstructural protein 5A from bovine viral diarrhea virus., Sapay N, Montserret R, Chipot C, Brass V, Moradpour D, Deleage G, Penin F, Biochemistry. 2006 Feb 21;45(7):2221-33. PMID:16475810

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