1cmv
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(New page: 200px<br /> <applet load="1cmv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmv, resolution 2.27Å" /> '''HUMAN CYTOMEGALOVIR...)
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Revision as of 18:08, 29 October 2007
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HUMAN CYTOMEGALOVIRUS PROTEASE
Overview
Herpesviruses encode a serine protease that specifically cleaves assembly, protein. This protease is critical for replication, and represents a new, target for antiviral drug design. Here we report the three-dimensional, structure of the protease from human cytomegalovirus (hCMV) at 2.27, angstroms resolution. The structure reveals a unique fold and new, catalytic strategy for cleavage. The monomer fold of the enzyme, a, seven-stranded beta-barrel encircled by a chain of helices that form the, carboxy terminus of the molecule, is unrelated to those observed in, classic serine proteases such as chymotrypsin and subtilisin. The serine, nucleophile at position 132 is activated by two juxtaposed histidine, residues at positions 63 and 157. Dimerization, which seems to be, necessary for ... [(full description)]
About this Structure
1CMV is a [Single protein] structure of sequence from [Human cytomegalovirus]. Full crystallographic information is available from [OCA].
Reference
Three-dimensional structure of human cytomegalovirus protease., Shieh HS, Kurumbail RG, Stevens AM, Stegeman RA, Sturman EJ, Pak JY, Wittwer AJ, Palmier MO, Wiegand RC, Holwerda BC, Stallings WC, Nature. 1996 Sep 19;383(6597):279-82. PMID:8805708
Page seeded by OCA on Mon Oct 29 20:12:46 2007
