The SAM domain of mouse SAMHD1 is critical for its activation and regulation

Olga Buzovetsky; Chenxiang Tang; Kirsten M. Knecht; Jenna M. Antonucci; Li Wu; Xiaoyun Ji; Yong Xiong

doi:10.1038/s41467-017-02783-8

Nature Communications (Jan 2018)

The SAM domain of mouse SAMHD1 is critical for its activation and regulation

Olga Buzovetsky,
Chenxiang Tang,
Kirsten M. Knecht,
Jenna M. Antonucci,
Li Wu,
Xiaoyun Ji,
Yong Xiong

Affiliations

Olga Buzovetsky: Department of Molecular Biophysics and Biochemistry, Yale University
Chenxiang Tang: Department of Molecular Biophysics and Biochemistry, Yale University
Kirsten M. Knecht: Department of Molecular Biophysics and Biochemistry, Yale University
Jenna M. Antonucci: Center of Retrovirus Research, Department of Veterinary Biosciences, The Ohio State University
Li Wu: Center of Retrovirus Research, Department of Veterinary Biosciences, The Ohio State University
Xiaoyun Ji: The State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing University
Yong Xiong: Department of Molecular Biophysics and Biochemistry, Yale University

DOI: https://doi.org/10.1038/s41467-017-02783-8
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 9

Abstract

Read online

The sterile alpha-motif and histidine-aspartate domain-containing protein 1 (SAMHD1) is a dNTP phosphohydrolase that blocks HIV-1 infection by depleting cellular dNTPs. Here the authors present the structures of full-length mouse SAMHD1 in different nucleotide bound states and give insights into SAMHD1 activity regulation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal