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PDBsum entry 1cb1
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Calcium-binding protein
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PDB id
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1cb1
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References listed in PDB file
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Key reference
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Title
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Three-Dimensional solution structure of ca(2+)-Loaded porcine calbindin d9k determined by nuclear magnetic resonance spectroscopy.
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Authors
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M.Akke,
T.Drakenberg,
W.J.Chazin.
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Ref.
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Biochemistry, 1992,
31,
1011-1020.
[DOI no: ]
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PubMed id
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Abstract
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The three-dimensional solution structure of native, intact porcine calbindin D9k
has been determined by distance geometry and restrained molecular dynamics
calculations using distance and dihedral angle constraints obtained from 1H NMR
spectroscopy. The protein has a well-defined global fold consisting of four
helices oriented in a pairwise antiparallel manner such that two pairs of
helix-loop-helix motifs (EF-hands) are joined by a linker segment. The two
EF-hands are further coupled through a short beta-type interaction between the
two Ca(2+)-binding loops. Overall, the structure is very similar to that of the
highly homologous native, minor A form of bovine calbindin D9k determined by
X-ray crystallography [Szebenyi, D. M. E., & Moffat, K. (1986) J. Biol.
Chem. 261, 8761-8776]. A model structure built from the bovine calbindin D9k
crystal structure shows several deviations larger than 2 A from the experimental
distance constraints for the porcine protein. These structural differences are
efficiently removed by subjecting the model structure to the experimental
distance and dihedral angle constraints in a restrained molecular dynamics
protocol, thereby generating a model that is very similar to the refined
distance geometry derived structures. The N-terminal residues of the intact
protein that are absent in the minor A form appear to be highly flexible and do
not influence the structure of other regions of the protein. This result is
important because it validates the conclusions drawn from the wide range of
studies that have been carried out on minor A forms rather than the intact
calbindin D9k.
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Secondary reference #1
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Title
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1h nmr studies of porcine calbindin d9k in solution: sequential resonance assignment, Secondary structure, And global fold.
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Authors
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T.Drakenberg,
T.Hofmann,
W.J.Chazin.
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Ref.
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Biochemistry, 1989,
28,
5946-5954.
[DOI no: ]
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PubMed id
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