This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1vzv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzv OCA], [http://www.ebi.ac.uk/pdbsum/1vzv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vzv RCSB]</span>
}}
}}
Line 35: Line 38:
[[Category: viral protease]]
[[Category: viral protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:50:15 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:29:11 2008''

Revision as of 21:29, 30 March 2008


PDB ID 1vzv

Drag the structure with the mouse to rotate
, resolution 3.0Å
Sites:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE


Overview

Varicella-zoster virus (VZV), an alpha-herpes virus, is the causative agent of chickenpox, shingles, and postherpetic neuralgia. The three-dimensional crystal structure of the serine protease from VZV has been determined at 3.0-A resolution. The VZV protease is essential for the life cycle of the virus and is a potential target for therapeutic intervention. The structure reveals an overall fold that is similar to that recently reported for the serine protease from cytomegalovirus (CMV), a herpes virus of the beta subfamily. The VZV protease structure provides further evidence to support the finding that herpes virus proteases have a fold and active site distinct from other serine proteases. The VZV protease catalytic triad consists of a serine and two histidines. The distal histidine is proposed to properly orient the proximal histidine. The identification of an alpha-helical segment in the VZV protease that was mostly disordered in the CMV protease provides a better definition of the postulated active site cavity and reveals an elastase-like S' region. Structural differences between the VZV and CMV proteases also suggest potential differences in their oligomerization states.

About this Structure

1VZV is a Single protein structure of sequence from Varicella-zoster virus (isolate 40a2). Full crystallographic information is available from OCA.

Reference

Crystal structure of varicella-zoster virus protease., Qiu X, Janson CA, Culp JS, Richardson SB, Debouck C, Smith WW, Abdel-Meguid SS, Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2874-9. PMID:9096314

Page seeded by OCA on Mon Mar 31 00:29:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools