1uk3: Difference between revisions
New page: left|200px<br /><applet load="1uk3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uk3, resolution 2.4Å" /> '''Crystal structure of ... |
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[[Image:1uk3.jpg|left|200px]]<br /><applet load="1uk3" size=" | [[Image:1uk3.jpg|left|200px]]<br /><applet load="1uk3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1uk3, resolution 2.4Å" /> | caption="1uk3, resolution 2.4Å" /> | ||
'''Crystal structure of SARS Coronavirus Main Proteinase (3CLpro) At pH7.6'''<br /> | '''Crystal structure of SARS Coronavirus Main Proteinase (3CLpro) At pH7.6'''<br /> | ||
==Overview== | ==Overview== | ||
A newly identified severe acute respiratory syndrome coronavirus | A newly identified severe acute respiratory syndrome coronavirus (SARS-CoV), is the etiological agent responsible for the outbreak of SARS. The SARS-CoV main protease, which is a 33.8-kDa protease (also called the 3C-like protease), plays a pivotal role in mediating viral replication and transcription functions through extensive proteolytic processing of two replicase polyproteins, pp1a (486 kDa) and pp1ab (790 kDa). Here, we report the crystal structures of the SARS-CoV main protease at different pH values and in complex with a specific inhibitor. The protease structure has a fold that can be described as an augmented serine-protease, but with a Cys-His at the active site. This series of crystal structures, which is the first, to our knowledge, of any protein from the SARS virus, reveal substantial pH-dependent conformational changes, and an unexpected mode of inhibitor binding, providing a structural basis for rational drug design. | ||
==About this Structure== | ==About this Structure== | ||
1UK3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http:// | 1UK3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UK3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bartlam, M.]] | [[Category: Bartlam, M.]] | ||
[[Category: Ding, Y.]] | [[Category: Ding, Y.]] | ||
[[Category: Gao, G | [[Category: Gao, G F.]] | ||
[[Category: Hilgenfeld, R.]] | [[Category: Hilgenfeld, R.]] | ||
[[Category: Liu, Y.]] | [[Category: Liu, Y.]] | ||
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[[Category: anti-parallel b-barrel]] | [[Category: anti-parallel b-barrel]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:26 2008'' | ||
Revision as of 16:25, 21 February 2008
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Crystal structure of SARS Coronavirus Main Proteinase (3CLpro) At pH7.6
OverviewOverview
A newly identified severe acute respiratory syndrome coronavirus (SARS-CoV), is the etiological agent responsible for the outbreak of SARS. The SARS-CoV main protease, which is a 33.8-kDa protease (also called the 3C-like protease), plays a pivotal role in mediating viral replication and transcription functions through extensive proteolytic processing of two replicase polyproteins, pp1a (486 kDa) and pp1ab (790 kDa). Here, we report the crystal structures of the SARS-CoV main protease at different pH values and in complex with a specific inhibitor. The protease structure has a fold that can be described as an augmented serine-protease, but with a Cys-His at the active site. This series of crystal structures, which is the first, to our knowledge, of any protein from the SARS virus, reveal substantial pH-dependent conformational changes, and an unexpected mode of inhibitor binding, providing a structural basis for rational drug design.
About this StructureAbout this Structure
1UK3 is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor., Yang H, Yang M, Ding Y, Liu Y, Lou Z, Zhou Z, Sun L, Mo L, Ye S, Pang H, Gao GF, Anand K, Bartlam M, Hilgenfeld R, Rao Z, Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13190-5. Epub 2003 Oct 29. PMID:14585926
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