Ontology highlight
ABSTRACT:
SUBMITTER: Li Y
PROVIDER: S-EPMC4705945 | biostudies-literature | 2015 Dec
REPOSITORIES: biostudies-literature
Li Yanhong Y Kong Jia J Peng Xin X Hou Wen W Qin Xiaohong X Yu Xiao-Fang XF
The Journal of biological chemistry 20151005 49
Sterile α-motif/histidine-aspartate domain-containing protein (SAMHD1), a homo-tetrameric GTP/dGTP-dependent dNTP triphosphohydrolase, catalyzes the conversion of dNTP into deoxynucleoside and triphosphate. As the only characterized dNTP triphosphohydrolase in human cells, SAMHD1 plays an important role in human innate immunity, autoimmunity, and cell cycle control. Previous biochemical studies and crystal structures have revealed that SAMHD1 interconverts between an inactive monomeric or dimeri ...[more]