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Literature summary for 2.1.1.45 extracted from

  • Chen, D.; Jansson, A.; Sim, D.; Larsson, A.; Nordlund, P.
    Structural analyses of human thymidylate synthase reveal a site that may control conformational switching between active and inactive states (2017), J. Biol. Chem., 292, 13449-13458 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
ligand-free, binary and ternary complex structures with phosphate ions and dUMP Homo sapiens

Protein Variants

Protein Variants Comment Organism
A191K inactive. Mutant has large areas of hydrophobic region exposed to solvent and exposes the hydrophobic beta-sheets in the dimer interface Homo sapiens
M190K inactive. Mutant has large areas of hydrophobic region exposed to solvent and exposes the hydrophobic beta-sheets in the dimer interface Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
nolatrexed upon binding, the two insert regions in thymidylate synthase, the functions of which are unclear, undergo positional shifts toward the catalytic center Homo sapiens
raltitrexed upon binding, the two insert regions in thymidylate synthase, the functions of which are unclear, undergo positional shifts toward the catalytic center Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P04818
-
-

Synonyms

Synonyms Comment Organism
TYMS
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function two insert regions in thymidylate synthase, the functions of which are unclear, are involved in the conformational transition between the active and inactive state. A cavity in the dimer interface could serve as an allosteric site to regulate the conformational switching between the active and inactive states Homo sapiens