Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2007 Jan 19;365(3):715-21.
doi: 10.1016/j.jmb.2006.10.030. Epub 2006 Oct 13.

Solution structure of the COMMD1 N-terminal domain

Monika Sommerhalter  1 , Yongbo Zhang, Amy C Rosenzweig
Affiliations

Solution structure of the COMMD1 N-terminal domain

Monika Sommerhalter et al. J Mol Biol. .

Abstract

COMMD1 is the prototype of a new protein family that plays a role in several important cellular processes, including NF-kappaB signaling, sodium transport, and copper metabolism. The COMMD proteins interact with one another via a conserved C-terminal domain, whereas distinct functions are predicted to result from a variable N-terminal domain. The COMMD proteins have not been characterized biochemically or structurally. Here, we present the solution structure of the N-terminal domain of COMMD1 (N-COMMD1, residues 1-108). This domain adopts an alpha-helical structure that bears little resemblance to any other helical protein. The compact nature of N-COMMD1 suggests that full-length COMMD proteins are modular, consistent with specific functional properties for each domain. Interactions between N-COMMD1 and partner proteins may occur via complementary electrostatic surfaces. These data provide a new foundation for biochemical characterization of COMMD proteins and for probing COMMD1 protein-protein interactions at the molecular level.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Stereoview of the 20 conformers representing the solution structure of N-COMMD1. The well-ordered regions comprise residues 9-19 and 30-101.
Figure 2
Figure 2
Ribbon diagram of the averaged and energy minimized structure of N-COMMD1 generated with PyMol. The N-terminus is colored in blue and the C-terminus in red.
Figure 3
Figure 3
Sequence alignment of human N-COMMD1 with its homologs from dog and mouse showing the secondary structure elements and the pattern of conserved residues. The amino acid sequences were obtained form Swiss-Prot (entries Q8N668, Q8WMD0, and Q8K4M5) and the alignment was generated with ClustalW.
Figure 4
Figure 4
Electrostatic surface of N-COMMD1 calculated with the programs PDB2PQR and APBS and displayed with PyMOL. The surface on the left corresponds to the orientation shown in Figure 2. The surface is color-coded according to electrostatic potential: red, -10 kT; white, 0 kT; blue, +10 kT.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Van De Sluis B, Rothuizen J, Pearson PL, Van Oost BA, Wijmenga C. Identification of a new copper metabolism gene by positional cloning in a purebred dog population. Hum Mol Genet. 2002;11:165–173. - PubMed
    1. Tao TY, Liu F, Klomp L, Wijmenga C, Gitlin JD. The copper toxicosis gene product Murr1 interacts directly with the Wilson disease protein. J Biol Chem. 2003;278:41593–41596. - PubMed
    1. Klomp AEM, Van De Sluis B, Klomp LWJ, Wijmenga C. The ubiquitously expressed Murr1 protein is absent in canine copper toxicosis. J Hepatol. 2003;39:703–709. - PubMed
    1. Hyun C, Filippich LC. Inherited canine copper toxicosis in Australian Bedlington Terriers. J Vet Sci. 2004;5:19–28. - PubMed
    1. Fuentealba IC, Aburto EM. Animal models of copper-associated liver disease. Comp Hepatol. 2003;2:5–17. - PMC - PubMed

Publication types

Associated data

LinkOut - more resources