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1zh1

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[[Image:1zh1.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1zh1", creates the "Structure Box" on the page.
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|GENE= Nonstructural protein 5A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11103 Hepatitis C virus])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zh1 OCA], [http://www.ebi.ac.uk/pdbsum/1zh1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zh1 RCSB]</span>
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'''Structure of the zinc-binding domain of HCV NS5A'''
'''Structure of the zinc-binding domain of HCV NS5A'''
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[[Category: Rice, C M.]]
[[Category: Rice, C M.]]
[[Category: Tellinghuisen, T L.]]
[[Category: Tellinghuisen, T L.]]
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[[Category: domain i]]
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[[Category: Domain i]]
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[[Category: hcv]]
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[[Category: Hcv]]
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[[Category: nonstructural protein 5a]]
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[[Category: Nonstructural protein 5a]]
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[[Category: ns5a]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:36:50 2008''
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Revision as of 14:36, 3 May 2008

Image:1zh1.gif

Template:STRUCTURE 1zh1

Structure of the zinc-binding domain of HCV NS5A


Overview

Hepatitis C virus (HCV) is a human pathogen affecting nearly 3% of the world's population. Chronic infections can lead to cirrhosis and liver cancer. The RNA replication machine of HCV is a multi-subunit membrane-associated complex. The non-structural protein NS5A is an active component of HCV replicase, as well as a pivotal regulator of replication and a modulator of cellular processes ranging from innate immunity to dysregulated cell growth. NS5A is a large phosphoprotein (56-58 kDa) with an amphipathic alpha-helix at its amino terminus that promotes membrane association. After this helix region, NS5A is organized into three domains. The N-terminal domain (domain I) coordinates a single zinc atom per protein molecule. Mutations disrupting either the membrane anchor or zinc binding of NS5A are lethal for RNA replication. However, probing the role of NS5A in replication has been hampered by a lack of structural information about this multifunctional protein. Here we report the structure of NS5A domain I at 2.5-A resolution, which contains a novel fold, a new zinc-coordination motif and a disulphide bond. We use molecular surface analysis to suggest the location of protein-, RNA- and membrane-interaction sites.

About this Structure

1ZH1 is a Single protein structure of sequence from Hepatitis c virus. Full crystallographic information is available from OCA.

Reference

Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase., Tellinghuisen TL, Marcotrigiano J, Rice CM, Nature. 2005 May 19;435(7040):374-9. PMID:15902263 Page seeded by OCA on Sat May 3 17:36:50 2008

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