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PDBsum entry 2nln
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Metal binding protein
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PDB id
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2nln
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Contents |
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* Residue conservation analysis
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DOI no:
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Protein Sci
16:1914-1926
(2007)
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PubMed id:
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Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin).
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M.T.Henzl,
J.J.Tanner.
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ABSTRACT
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Relative to other parvalbumin isoforms, the mammalian beta-parvalbumin
(oncomodulin) displays attenuated divalent ion affinity. High-resolution
structural data for the Ca(2+)-bound protein have provided little insight into
the physical basis for this behavior, prompting an examination of the unliganded
state. This article describes the solution structure and peptide backbone
dynamics of Ca(2+)-free rat beta-parvalbumin (beta-PV). Ca(2+) removal evidently
provokes significant structural alterations. Interaction between the D helix and
the AB domain in the Ca(2+)-bound protein is greatly diminished in the apo-form,
permitting the D helix to straighten. There is also a significant reorganization
of the hydrophobic core and a concomitant remodeling of the interface between
the AB and CD-EF domains. These modifications perturb the orientation of the C
and D helices, and the energetic penalty associated with their reversal could
contribute to the low-affinity signature of the CD site. By contrast, Ca(2+)
removal causes a comparatively minor perturbation of the E and F helices,
consistent with the more typical divalent ion affinity observed for the EF site.
Ca(2+)-free rat beta-PV retains structural rigidity on the picosecond-nanosecond
timescale. At 20 degrees C, the majority of amide vectors show no evidence for
motion on timescales above 20 ps, and the average order parameter for the entire
molecule is 0.92.
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Selected figure(s)
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Figure 6.
Figure 6. Ca
2+
removal modifies hydrophobic contacts in the AB domain.
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The above figure is
reprinted
by permission from the Protein Society:
Protein Sci
(2007,
16,
1914-1926)
copyright 2007.
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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.T.Henzl,
J.J.Tanner,
and
A.Tan
(2011).
Solution structures of chicken parvalbumin 3 in the Ca(2+)-free and Ca(2+)-bound states.
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Proteins,
79,
752-764.
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PDB codes:
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D.D.Simmons,
B.Tong,
A.D.Schrader,
and
A.J.Hornak
(2010).
Oncomodulin identifies different hair cell types in the mammalian inner ear.
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J Comp Neurol,
518,
3785-3802.
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J.P.Schuermann,
A.Tan,
J.J.Tanner,
and
M.T.Henzl
(2010).
Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states.
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J Mol Biol,
397,
991.
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PDB codes:
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B.A.Tikunov,
and
L.C.Rome
(2009).
Is high concentration of parvalbumin a requirement for superfast relaxation?
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J Muscle Res Cell Motil,
30,
57-65.
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M.T.Henzl,
and
J.J.Tanner
(2008).
Solution structure of Ca2+-free rat alpha-parvalbumin.
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Protein Sci,
17,
431-438.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
