Description
Experimental Technique/Method:SOLUTION NMR
Resolution:
Classification:METAL TRANSPORT
Release Date:2006-12-05
Deposition Date:2006-05-19
Revision Date:2008-05-01#2011-07-13
Molecular Weight:11910.6
Macromolecule Type:Protein
Residue Count:108
Atom Site Count:837
DOI:10.2210/pdb2h2m/pdb
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.
Resolution:
Classification:METAL TRANSPORT
Release Date:2006-12-05
Deposition Date:2006-05-19
Revision Date:2008-05-01#2011-07-13
Molecular Weight:11910.6
Macromolecule Type:Protein
Residue Count:108
Atom Site Count:837
DOI:10.2210/pdb2h2m/pdb
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.
| Date made available | 2006 |
|---|---|
| Publisher | RCSB-PDB |