1fl1
From Proteopedia
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KSHV PROTEASE
Overview
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.
About this Structure
1FL1 is a Single protein structure of sequence from Human herpesvirus 4 with K as ligand. 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
Page seeded by OCA on Sat Nov 24 23:59:04 2007
