Structural analyses of human thymidylate synthase reveal a site that may control conformational switching between active and inactive states

• المؤلفون الرئيسيون: Chen, Dan, Jansson, Anna, Sim, Daniel, Larsson, Andreas, Nordlund, Pär
• مؤلفون آخرون: School of Biological Sciences
• التنسيق: مقال
• اللغة: English
• منشور في: 2018
• الموضوعات: Crystallography; Conformational Change; DRNTU::Science::Biological sciences
• الوصول للمادة أونلاين: https://hdl.handle.net/10356/87827; http://hdl.handle.net/10220/46834

Thymidylate synthase (TS) is the sole enzyme responsible for de novo biosynthesis of thymidylate (TMP) and is essential for cell proliferation and survival. Inhibition of human TS (hTS) has been extensively investigated for cancer chemotherapy, but several aspects of its activity and regulation are...