1at3

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[[Image:1at3.gif|left|200px]]<br /><applet load="1at3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1at3.gif|left|200px]]
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caption="1at3, resolution 2.5&Aring;" />
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'''HERPES SIMPLEX VIRUS TYPE II PROTEASE'''<br />
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{{Structure
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|PDB= 1at3 |SIZE=350|CAPTION= <scene name='initialview01'>1at3</scene>, resolution 2.5&Aring;
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|SITE= <scene name='pdbsite=ACT:Novel+Active+Site+Triad+SER+129,+HIS+61+And+HIS+148'>ACT</scene>
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|LIGAND= <scene name='pdbligand=DFP:DIISOPROPYL PHOSPHONATE'>DFP</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''HERPES SIMPLEX VIRUS TYPE II PROTEASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1AT3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1] with <scene name='pdbligand=DFP:'>DFP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=ACT:Novel+Active+Site+Triad+SER+129,+HIS+61+And+HIS+148'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AT3 OCA].
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1AT3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AT3 OCA].
==Reference==
==Reference==
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Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex., Hoog SS, Smith WW, Qiu X, Janson CA, Hellmig B, McQueney MS, O'Donnell K, O'Shannessy D, DiLella AG, Debouck C, Abdel-Meguid SS, Biochemistry. 1997 Nov 18;36(46):14023-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9369473 9369473]
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Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex., Hoog SS, Smith WW, Qiu X, Janson CA, Hellmig B, McQueney MS, O'Donnell K, O'Shannessy D, DiLella AG, Debouck C, Abdel-Meguid SS, Biochemistry. 1997 Nov 18;36(46):14023-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9369473 9369473]
[[Category: Human herpesvirus 1]]
[[Category: Human herpesvirus 1]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: viral protease]]
[[Category: viral protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:01:55 2008''

Revision as of 08:01, 20 March 2008


PDB ID 1at3

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, resolution 2.5Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



HERPES SIMPLEX VIRUS TYPE II PROTEASE


Overview

Human herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) are responsible for herpes labialis (cold sores) and genital herpes, respectively. They encode a serine protease that is required for viral replication, and represent a viable target for therapeutic intervention. Here, we report the crystal structures of HSV-1 and HSV-2 proteases, the latter in the presence and absence of the covalently bound transition state analog inhibitor diisopropyl phosphate (DIP). The HSV-1 and HSV-2 protease structures show a fold that is neither like chymotrypsin nor like subtilisin, and has been seen only in the recently determined cytomegalovirus (CMV) and varicella-zoster virus (VZV) protease structures. HSV-1 and HSV-2 proteases share high sequence homology and have almost identical three-dimensional structures. However, structural differences are observed with the less homologous CMV protease, offering a structural basis for herpes virus protease ligand specificity. The bound inhibitor identifies the oxyanion hole of these enzymes and defines the active site cavity.

About this Structure

1AT3 is a Single protein structure of sequence from Human herpesvirus 1. Full crystallographic information is available from OCA.

Reference

Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex., Hoog SS, Smith WW, Qiu X, Janson CA, Hellmig B, McQueney MS, O'Donnell K, O'Shannessy D, DiLella AG, Debouck C, Abdel-Meguid SS, Biochemistry. 1997 Nov 18;36(46):14023-9. PMID:9369473

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