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






3 Functional Relationships(s)
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1 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. 2'-deoxyadenosine triphosphate SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens
2 In addition, we present biochemical analyses of GTP-induced SAMHD1 full-length tetramerization and the structure of SAMHD1 catalytic core tetramer in complex with GTP/dATP, revealing the structural basis of GTP-mediated SAMHD1 activation. 2'-deoxyadenosine triphosphate SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens
3 In addition, we present biochemical analyses of GTP-induced SAMHD1 full-length tetramerization and the structure of SAMHD1 catalytic core tetramer in complex with GTP/dATP, revealing the structural basis of GTP-mediated SAMHD1 activation. 2'-deoxyadenosine triphosphate SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 Homo sapiens