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Title: Region directed mutagenesis of Varicella-zoster virus thymidylate synthase
Author: Boffey, Judith
ISNI:       0000 0001 3468 9238
Awarding Body: University of Glasgow
Current Institution: University of Glasgow
Date of Award: 1998
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Thymidylate synthase (TS) catalyses the reductive methylation of deoxyuridine monophosphate by 5,10-methylenetetrahydrofolate to produce thymidylate and dihydrofolate. In the reaction the enzyme is present initially as an open complex that closes down progressively as ligands bind. The binary complex which is formed as the substrate dUMP binds has an active site that is open and structurally very close to the unliganded state. It is upon binding of the folate cofactor that structural changes occur and the enzyme forms a closed ternary structure. In contrast to the movements of large domains seen in other proteins upon ligand binding, the changes in TS involves segmental accommodation in which segments of secondary structural elements all move in concert towards the active site. The two largest shifts involve the C-terminus and DRTG loop which moves 4A to close over the active site.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available
Keywords: Herpesvirus