2h2m
Solution Structure of the N-terminal domain of COMMD1 (Murr1)
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OverviewOverview
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.
About this StructureAbout this Structure
2H2M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the COMMD1 N-terminal domain., Sommerhalter M, Zhang Y, Rosenzweig AC, J Mol Biol. 2007 Jan 19;365(3):715-21. Epub 2006 Oct 13. PMID:17097678
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