Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 Oct 5;290(49):29428–29437. doi: 10.1074/jbc.M115.663658

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

PMC Copyright notice

FIGURE 3. — The interface between the A and C subunits is essential for the tetramer formation of SAMHD1C. A, mutations of residues involved in the interactions between subunits A and C of SAMHD1 affect tetramer formation. Purified recombinant SAMHD1C and SAMHD1C mutant proteins were incubated with 50 mm dGTP and separated by size-exclusion chromatography. The elution profiles were monitored by ultraviolet absorbance at A₂₈₀ and compared with known molecular size markers. mAU, milliabsorbance units. B, mutations of residues involved the interactions between subunits A and C of SAMHD1C affect dNTPase activity. Purified recombinant SAMHD1C and SAMHD1C mutant proteins were analyzed for dNTPase activity as described under “Experimental Procedures,” and the activity of SAMHD1C was set to 100%. The S.D. from triplicate samples (n = 3) is shown.