1p9u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1p9u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9u, resolution 2.37&Aring;" /> '''Coronavirus Main Pro...)
Line 1: Line 1:
-
[[Image:1p9u.gif|left|200px]]<br /><applet load="1p9u" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1p9u.gif|left|200px]]<br /><applet load="1p9u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p9u, resolution 2.37&Aring;" />
caption="1p9u, resolution 2.37&Aring;" />
'''Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of anti-SARS Drugs'''<br />
'''Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of anti-SARS Drugs'''<br />
==Overview==
==Overview==
-
A novel coronavirus has been identified as the causative agent of severe, acute respiratory syndrome (SARS). The viral main proteinase (Mpro, also, called 3CLpro), which controls the activities of the coronavirus, replication complex, is an attractive target for therapy. We determined, crystal structures for human coronavirus (strain 229E) Mpro and for an, inhibitor complex of porcine coronavirus [transmissible gastroenteritis, virus (TGEV)] Mpro, and we constructed a homology model for SARS, coronavirus (SARS-CoV) Mpro. The structures reveal a remarkable degree of, conservation of the substrate-binding sites, which is further supported by, recombinant SARS-CoV Mpro-mediated cleavage of a TGEV Mpro substrate., Molecular modeling suggests that available rhinovirus 3Cpro inhibitors may, be modified to make them useful for treating SARS.
+
A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (Mpro, also called 3CLpro), which controls the activities of the coronavirus replication complex, is an attractive target for therapy. We determined crystal structures for human coronavirus (strain 229E) Mpro and for an inhibitor complex of porcine coronavirus [transmissible gastroenteritis virus (TGEV)] Mpro, and we constructed a homology model for SARS coronavirus (SARS-CoV) Mpro. The structures reveal a remarkable degree of conservation of the substrate-binding sites, which is further supported by recombinant SARS-CoV Mpro-mediated cleavage of a TGEV Mpro substrate. Molecular modeling suggests that available rhinovirus 3Cpro inhibitors may be modified to make them useful for treating SARS.
==About this Structure==
==About this Structure==
-
1P9U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Transmissible_gastroenteritis_virus Transmissible gastroenteritis virus] with SO4, CH2 and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P9U OCA].
+
1P9U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Transmissible_gastroenteritis_virus Transmissible gastroenteritis virus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CH2:'>CH2</scene> and <scene name='pdbligand=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9U OCA].
==Reference==
==Reference==
Line 15: Line 15:
[[Category: Anand, K.]]
[[Category: Anand, K.]]
[[Category: Hilgenfeld, R.]]
[[Category: Hilgenfeld, R.]]
-
[[Category: Mesters, J.R.]]
+
[[Category: Mesters, J R.]]
[[Category: Wadhwani, P.]]
[[Category: Wadhwani, P.]]
[[Category: Ziebuhr, J.]]
[[Category: Ziebuhr, J.]]
Line 26: Line 26:
[[Category: tgev]]
[[Category: tgev]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:37:17 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:39 2008''

Revision as of 12:26, 21 February 2008

Image:1p9u.gif

1p9u, resolution 2.37Å

Drag the structure with the mouse to rotate

Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of anti-SARS Drugs

Overview

A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (Mpro, also called 3CLpro), which controls the activities of the coronavirus replication complex, is an attractive target for therapy. We determined crystal structures for human coronavirus (strain 229E) Mpro and for an inhibitor complex of porcine coronavirus [transmissible gastroenteritis virus (TGEV)] Mpro, and we constructed a homology model for SARS coronavirus (SARS-CoV) Mpro. The structures reveal a remarkable degree of conservation of the substrate-binding sites, which is further supported by recombinant SARS-CoV Mpro-mediated cleavage of a TGEV Mpro substrate. Molecular modeling suggests that available rhinovirus 3Cpro inhibitors may be modified to make them useful for treating SARS.

About this Structure

1P9U is a Single protein structure of sequence from Transmissible gastroenteritis virus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs., Anand K, Ziebuhr J, Wadhwani P, Mesters JR, Hilgenfeld R, Science. 2003 Jun 13;300(5626):1763-7. Epub 2003 May 13. PMID:12746549

Page seeded by OCA on Thu Feb 21 14:26:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p9u"
Personal tools