1FL1
KSHV PROTEASE
Summary for 1FL1
| Entry DOI | 10.2210/pdb1fl1/pdb |
| Related | 1AT3 1CMV 1LAY 1VZV 1WPO |
| Descriptor | PROTEASE, POTASSIUM ION (3 entities in total) |
| Functional Keywords | serine protease, antiviral drug design, capsid maturation, endopeptidase, assemblin, viral protein |
| Biological source | Human herpesvirus 8 |
| Total number of polymer chains | 2 |
| Total formula weight | 50498.97 |
| Authors | Reiling, K.K.,Pray, T.R.,Craik, C.S.,Stroud, R.M. (deposition date: 2000-08-11, release date: 2000-11-22, Last modification date: 2024-02-07) |
| Primary citation | Reiling, K.K.,Pray, T.R.,Craik, C.S.,Stroud, R.M. Functional consequences of the Kaposi's sarcoma-associated herpesvirus protease structure: regulation of activity and dimerization by conserved structural elements. Biochemistry, 39:12796-12803, 2000 Cited by PubMed Abstract: 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. PubMed: 11041844DOI: 10.1021/bi001019h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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