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TitleStructural and functional characterization explains loss of dNTPase activity of the cancer-specific R366C/H mutant SAMHD1 proteins.
Journal, issue, pagesJ. Biol. Chem., Vol. 297, Page 101170-101170, Year 2021
Publish dateFeb 20, 2021 (structure data deposition date)
AuthorsBowen, N.E. / Temple, J. / Shepard, C. / Oo, A. / Arizaga, F. / Kapoor-Vazirani, P. / Persaud, M. / Yu, C.H. / Kim, D.H. / Schinazi, R.F. ...Bowen, N.E. / Temple, J. / Shepard, C. / Oo, A. / Arizaga, F. / Kapoor-Vazirani, P. / Persaud, M. / Yu, C.H. / Kim, D.H. / Schinazi, R.F. / Ivanov, D.N. / Diaz-Griffero, F. / Yu, D.S. / Xiong, Y. / Kim, B.
External linksJ. Biol. Chem. / PubMed:34492268
MethodsX-ray diffraction
Resolution1.9 - 3.57 Å
Structure data

PDB-7ltt:
SAMHD1(113-626) H206R D207N R366C
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-7lu5:
SAMHD1(113-626) H206R D207N R366H
Method: X-RAY DIFFRACTION / Resolution: 3.57 Å

Chemicals

ChemComp-DGT:
2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / dNTPase / tetramer / mutant / cancer

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