Title : Structural basis of allosteric activation of sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) by nucleoside triphosphates.

Pub. Date : 2014 Nov 21

PMID : 25288794






2 Functional Relationships(s)
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1 Recent structural data suggested a compelling mechanism for the regulation of SAMHD1 enzymatic activity and revealed dGTP-induced association of two inactive dimers into an active tetrameric enzyme. deoxyguanosine triphosphate SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens
2 Here, we present the crystal structures of SAMHD1 catalytic core (residues 113-626) tetramers, complexed with mixtures of nucleotides, including dGTP/dATP, dGTP/dCTP, dGTP/dTTP, and dGTP/dUTP. deoxyguanosine triphosphate SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens