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Literature summary for 2.4.2.4 extracted from

  • Norman, R.A.; Barry, S.T.; Bate, M.; Breed, J.; Colls, J.G.; Ernill, R.J.; Luke, R.W.; Minshull, C.A.; McAlister, M.S.; McCall, E.J.; McMiken, H.H.; Paterson, D.S.; Timms, D.; Tucker, J.A.; Pauptit, R.A.
    Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor (2004), Structure, 12, 75-84.
    View publication on PubMed
Search for more literature for 2.4.2.4

Application

Application Comment Organism
medicine structural insight into the binding mode of the inhibitor to this important drug target forms the basis for designing novel inhibitors for use in anticancer therapy Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of HTP bound to the small molecule inhibitor 5-chloro-6-[1-(2-iminopyrrolidinyl)methyl]uracil hydrochloride, glutathione S-transferase fused to thymidine phosphorylase residues 12–482 (based on Swissprot accession number P19971) via a thrombin-cleavable linker, crystallizationd at 15°C using the hanging-drop vapor method Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
5-chloro-6-[1-(2-iminopyrrolidinyl) methyl] uracil hydrochloride
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P19971
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
HTP
-
 Homo sapiens
platelet-derived endothelial cell growth factor
-
 Homo sapiens