1QHI

HERPES SIMPLEX VIRUS TYPE-I THYMIDINE KINASE COMPLEXED WITH A NOVEL NON-SUBSTRATE INHIBITOR, 9-(4-HYDROXYBUTYL)-N2-PHENYLGUANINE

Summary for 1QHI

• Entry DOI: 10.2210/pdb1qhi/pdb
• Descriptor: PROTEIN (THYMIDINE KINASE), SULFATE ION, 9-(4-HYDROXYBUTYL)-N2-PHENYLGUANINE, ... (4 entities in total)
• Functional Keywords: transferase, transferase (phosphotransferase) thymidine, transferase (phosphotransferase) thymidine kinase; viridae; ds-dna enveloped viruses; herpesviridae; alphaherpesvirinae novel inhibitor
• Biological source: Herpes simplex virus (type 1 / strain 17)
• Total number of polymer chains: 2
• Total formula weight: 80569.97

Authors

Bennett, M.S.,Wien, F.,Champness, J.N.,Batuwangala, T.,Rutherford, T.,Summers, W.C.,Sun, H.,Wright, G.,Sanderson, M.R. (deposition date: 1999-05-12, release date: 1999-07-09, Last modification date: 2023-08-16)

Primary citation

Bennett, M.S.,Wien, F.,Champness, J.N.,Batuwangala, T.,Rutherford, T.,Summers, W.C.,Sun, H.,Wright, G.,Sanderson, M.R.
Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir.
FEBS Lett., 443:121-125, 1999

PubMed Abstract: Treatment of herpes infections with nucleoside analogues requires as an initial step the activation of the compounds by thymidine kinase. As an aid to developing more effective chemotherapy, both for treatment of recurrent herpes infection and in gene therapy systems where thymidine kinase is expressed, two high-resolution X-ray structures of thymidine kinase have been compared: one with the relatively poor substrate aciclovir (Zovirax), the other with a synthetic inhibitor having an N2-substituted guanine. Both compounds have similar binding modes in spite of their size difference and apparently distinct ligand properties.

PubMed: 9989588
DOI: 10.1016/S0014-5793(98)01619-6

Experimental method

X-RAY DIFFRACTION (1.9 Å)