1zh1
From Proteopedia
(New page: 200px<br /><applet load="1zh1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zh1, resolution 2.5Å" /> '''Structure of the zinc...) |
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| - | [[Image:1zh1.gif|left|200px]]<br /><applet load="1zh1" size=" | + | [[Image:1zh1.gif|left|200px]]<br /><applet load="1zh1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zh1, resolution 2.5Å" /> | caption="1zh1, resolution 2.5Å" /> | ||
'''Structure of the zinc-binding domain of HCV NS5A'''<br /> | '''Structure of the zinc-binding domain of HCV NS5A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hepatitis C virus (HCV) is a human pathogen affecting nearly 3% of the | + | 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== | ==About this Structure== | ||
| - | 1ZH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ZH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZH1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Marcotrigiano, J.]] | [[Category: Marcotrigiano, J.]] | ||
| - | [[Category: Rice, C | + | [[Category: Rice, C M.]] |
| - | [[Category: Tellinghuisen, T | + | [[Category: Tellinghuisen, T L.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: domain i]] | [[Category: domain i]] | ||
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[[Category: ns5a]] | [[Category: ns5a]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:29 2008'' |
Revision as of 14:15, 21 February 2008
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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 with as ligand. 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
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