1fl1

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{{STRUCTURE_1fl1| PDB=1fl1 | SCENE= }}
{{STRUCTURE_1fl1| PDB=1fl1 | SCENE= }}
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'''KSHV PROTEASE'''
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===KSHV PROTEASE===
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==Overview==
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The structure of Kaposi's sarcoma-associated herpesvirus protease (KSHV Pr), at 2.2 A resolution, reveals the active-site geometry and defines multiple possible target sites for drug design against a human cancer-producing virus. The catalytic triad of KSHV Pr, (Ser114, His46, and His157) and transition-state stabilization site are arranged as in other structurally characterized herpesviral proteases. The distal histidine-histidine hydrogen bond is solvent accessible, unlike the situation in other classes of serine proteases. As in all herpesviral proteases, the enzyme is active only as a weakly associated dimer (K(d) approximately 2 microM), and inactive as a monomer. Therefore, both the active site and dimer interface are potential targets for antiviral drug design. The dimer interface in KSHV Pr is compared with the interface of other herpesviral proteases. Two conserved arginines (Arg209), one from each monomer, are buried within the same region of the dimer interface. We propose that this conserved arginine may provide a destabilizing element contributing to the tuned micromolar dissociation of herpesviral protease dimers.
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(as it appears on PubMed at http://www.pubmed.gov), where 11041844 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11041844}}
==About this Structure==
==About this Structure==
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[[Category: Endopeptidase]]
[[Category: Endopeptidase]]
[[Category: Serine protease]]
[[Category: Serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:27:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:25:33 2008''

Revision as of 00:25, 1 July 2008

Image:1fl1.png

Template:STRUCTURE 1fl1

KSHV PROTEASE

Template:ABSTRACT PUBMED 11041844

About this Structure

1FL1 is a Single protein structure of sequence from Human herpesvirus 8. Full crystallographic information is available from OCA.

Reference

Functional consequences of the Kaposi's sarcoma-associated herpesvirus protease structure: regulation of activity and dimerization by conserved structural elements., Reiling KK, Pray TR, Craik CS, Stroud RM, Biochemistry. 2000 Oct 24;39(42):12796-803. PMID:11041844

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