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'''Solution Structure of the N-terminal domain of COMMD1 (Murr1)''' | '''Solution Structure of the N-terminal domain of COMMD1 (Murr1)''' | ||
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[[Category: Sommerhalter, M.]] | [[Category: Sommerhalter, M.]] | ||
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
[[Category: | [[Category: All alpha-helical]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:47:49 2008'' | |||
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Revision as of 02:47, 4 May 2008
Solution Structure of the N-terminal domain of COMMD1 (Murr1)
Overview
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 Structure
2H2M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 05:47:49 2008
