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TitleHotspots in an obligate homodimeric anticancer target. Structural and functional effects of interfacial mutations in human thymidylate synthase.
Journal, issue, pagesJ. Med. Chem., Vol. 58, Page 3572-3581, Year 2015
Publish dateFeb 26, 2013 (structure data deposition date)
AuthorsSalo-Ahen, O.M. / Tochowicz, A. / Pozzi, C. / Cardinale, D. / Ferrari, S. / Boum, Y. / Mangani, S. / Stroud, R.M. / Saxena, P. / Myllykallio, H. ...Salo-Ahen, O.M. / Tochowicz, A. / Pozzi, C. / Cardinale, D. / Ferrari, S. / Boum, Y. / Mangani, S. / Stroud, R.M. / Saxena, P. / Myllykallio, H. / Costi, M.P. / Ponterini, G. / Wade, R.C.
External linksJ. Med. Chem. / PubMed:25798950
MethodsX-ray diffraction
Resolution2.03 - 2.311 Å
Structure data

PDB-4jef:
Crystal structure of human thymidylate synthase Y202A in inactive conformation.
Method: X-RAY DIFFRACTION / Resolution: 2.311 Å

PDB-4kpw:
Crystal structure of His-tagged human thymidylate synthase R175A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.03 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Inactive form of human thymidylate synthase / hot spot residue / interface hot spot / METHYLTRANSFERASE / NUCLEOTIDE BIOSYNTHESIS

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