2H2M

Solution Structure of the N-terminal domain of COMMD1 (Murr1)

Summary for 2H2M

• Entry DOI: 10.2210/pdb2h2m/pdb
• Descriptor: COMM domain-containing protein 1 (1 entity in total)
• Functional Keywords: all alpha-helical, metal transport
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q8N668
• Total number of polymer chains: 1
• Total formula weight: 11910.60

Authors

Sommerhalter, M.,Zhang, Y.,Rosenzweig, A.C. (deposition date: 2006-05-19, release date: 2006-12-05, Last modification date: 2024-05-29)

Primary citation

Sommerhalter, M.,Zhang, Y.,Rosenzweig, A.C.
Solution Structure of the COMMD1 N-terminal Domain.
J.Mol.Biol., 365:715-721, 2007

PubMed 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: 17097678
DOI: 10.1016/j.jmb.2006.10.030

Experimental method

SOLUTION NMR