Ontology highlight
ABSTRACT:
SUBMITTER: Koharudin LM
PROVIDER: S-EPMC4239615 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Koharudin Leonardus M I LM Wu Ying Y DeLucia Maria M Mehrens Jennifer J Gronenborn Angela M AM Ahn Jinwoo J
The Journal of biological chemistry 20141006 47
Sterile α motif and histidine-aspartate domain-containing protein 1 (SAMHD1) plays a critical role in inhibiting HIV infection, curtailing the pool of dNTPs available for reverse transcription of the viral genome. 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. Here, we present the crystal structures of SAMHD1 catalytic core (residues 113-626) tet ...[more]