2h2m
From Proteopedia
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| - | [[Image:2h2m.gif|left|200px]] | + | [[Image:2h2m.gif|left|200px]] |
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| - | '''Solution Structure of the N-terminal domain of COMMD1 (Murr1)''' | + | {{Structure |
| + | |PDB= 2h2m |SIZE=350|CAPTION= <scene name='initialview01'>2h2m</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= COMMD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Solution Structure of the N-terminal domain of COMMD1 (Murr1)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2H2M is a [ | + | 2H2M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H2M OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17097678 17097678] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: all alpha-helical]] | [[Category: all alpha-helical]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:11:51 2008'' |
Revision as of 15:11, 20 March 2008
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| Gene: | COMMD1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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