Modeling functional changes to Escherichia coli thymidylate synthase upon single residue replacements: a structure-based approach
Escherichia coli thymidylate synthase (TS) is an enzyme that is indispensable to DNA synthesis and cell division, as it provides the only de novo source of dTMP by catalyzing the reductive methylation of dUMP, thus making it a key target for chemotherapeutic agents. High resolution X-ray crystallogr...
Main Author: | Majid Masso |
---|---|
Format: | Article |
Language: | English |
Published: |
PeerJ Inc.
2015-01-01
|
Series: | PeerJ |
Subjects: | |
Online Access: | https://peerj.com/articles/721.pdf |
Similar Items
-
Alvaxanthone, a Thymidylate Synthase Inhibitor with Nematocidal and Tumoricidal Activities
by: Piotr Maj, et al.
Published: (2020-06-01) -
Evidence of Destabilization of the Human Thymidylate Synthase (hTS) Dimeric Structure Induced by the Interface Mutation Q62R
by: Cecilia Pozzi, et al.
Published: (2019-04-01) -
Thymidylate synthase inhibitors for thoracic tumors
by: Peters Godefridus J., et al.
Published: (2013-06-01) -
Mechanistic and structural basis for inhibition of thymidylate synthase ThyX
by: Tamara Basta, et al.
Published: (2012-01-01) -
Dynamic allostery in substrate binding by human thymidylate synthase
by: Jeffrey P Bonin, et al.
Published: (2022-10-01)