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PDBsum entry 2h2m
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Metal transport
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PDB id
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2h2m
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References listed in PDB file
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Key reference
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Title
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Solution structure of the commd1 n-Terminal domain.
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Authors
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M.Sommerhalter,
Y.Zhang,
A.C.Rosenzweig.
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Ref.
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J Mol Biol, 2007,
365,
715-721.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. Stereoview of the 20 conformers representing the
solution structure of N-COMMD1. The well-ordered regions
comprise residues 9–19 and 30–101. Figure 1. Stereoview
of the 20 conformers representing the solution structure of
N-COMMD1. The well-ordered regions comprise residues 9–19 and
30–101.
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Figure 2.
Figure 2. Ribbon diagram of the averaged and energy minimized
structure of N-COMMD1 generated with PyMOL
[http://pymol.sourceforge.net/]. The N-terminus is colored in
blue and the C-terminus in red. Figure 2. Ribbon diagram of
the averaged and energy minimized structure of N-COMMD1
generated with PyMOL [http://pymol.sourceforge.net/]. The
N-terminus is colored in blue and the C-terminus in red.
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The above figures are
reprinted
from an Open Access publication published by Elsevier:
J Mol Biol
(2007,
365,
715-721)
copyright 2007.
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