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PDBsum entry 1jwd
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Metal binding protein
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PDB id
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1jwd
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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A structural basis for s100 protein specificity derived from comparative analysis of apo and ca(2+)-Calcyclin.
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Authors
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L.Mäler,
M.Sastry,
W.J.Chazin.
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Ref.
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J Mol Biol, 2002,
317,
279-290.
[DOI no: ]
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PubMed id
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Abstract
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Calcyclin is a homodimeric protein belonging to the S100 subfamily of EF-hand
Ca(2+)-binding proteins, which function in Ca(2+) signal transduction processes.
A refined high-resolution solution structure of Ca(2+)-bound rabbit calcyclin
has been determined by heteronuclear solution NMR. In order to understand the
Ca(2+)-induced structural changes in S100 proteins, in-depth comparative
structural analyses were used to compare the apo and Ca(2+)-bound states of
calcyclin, the closely related S100B, and the prototypical Ca(2+)-sensor protein
calmodulin. Upon Ca(2+) binding, the position and orientation of helix III in
the second EF-hand is altered, whereas the rest of the protein, including the
dimer interface, remains virtually unchanged. This Ca(2+)-induced structural
change is much less drastic than the "opening" of the globular EF-hand
domains that occurs in classical Ca(2+) sensors, such as calmodulin. Using
homology models of calcyclin based on S100B, a binding site in calcyclin has
been proposed for the N-terminal domain of annexin XI and the C-terminal domain
of the neuronal calcyclin-binding protein. The structural basis for the
specificity of S100 proteins is discussed in terms of the variation in sequence
of critical contact residues in the common S100 target-binding site.
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Figure 3.
Figure 3. Ca
2+
-induced changes in the side-chain
packing of calcyclin. Overlay of the ensemble of apo
and Ca
2+
-bound calcyclin structures showing side-
chains involved in the interfaces between (a) helices I
and IV and (b) helices III and IV. The apo protein is
blue and the Ca
2+
-bound state is red.
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Figure 4.
Figure 4. Comparison of the Ca
2+
-induced structural
changes in calcyclin and S100B, and the N-terminal
domain of calmodulin. Apo structures are shown in
blue and Ca
2+
-loaded structures in red. Superpositions
were made using all backbone atoms. The left-hand
panel shows the changes in the N-terminal EF-hand and
the right-hand panel shows the changes in the C-term-
inal EF-hand of (a) calcyclin, (b) S100B, and (c) calmodu-
lin.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2002,
317,
279-290)
copyright 2002.
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Secondary reference #1
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Title
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High resolution solution structure of apo calcyclin and structural variations in the s100 family of calcium-Binding proteins.
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Authors
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L.Mäler,
B.C.Potts,
W.J.Chazin.
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Ref.
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J Biomol Nmr, 1999,
13,
233-247.
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PubMed id
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Secondary reference #2
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Title
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The three-Dimensional structure of ca(2+)-Bound calcyclin: implications for ca(2+)-Signal transduction by s100 proteins.
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Authors
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M.Sastry,
R.R.Ketchem,
O.Crescenzi,
C.Weber,
M.J.Lubienski,
H.Hidaka,
W.J.Chazin.
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Ref.
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Structure, 1998,
6,
223-231.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2. Comparison of the three-dimensional structures of
calcyclin and calbindin D[9k] in the Ca^2+-bound state. Overview
of calbindin D[9k] (a) and the calcyclin subunit (b),
highlighting the conserved residues in the hydrophobic core
(cyan). The two structures were first overlaid by best-fit
superposition of the backbone atoms of helices I, II and IV,
then separated for viewing. (c) Stereo close-up view of the
conserved hydrophobic residues at the interface between helices
I and IV, showing the similarity in the packing of corresponding
sidechains. The structures were overlaid by best-fit
superposition of the backbone atoms of helices I and IV.
Calbindin D[9k] is shown in yellow and calcyclin is in salmon;
the sidechains are labeled for calcyclin only. The coordinates
for calbindin D[9k] were obtained from the Brookhaven PDB
(accession code 2BCB). (Figure prepared using Insight II
[Version 95.0; MSI, San Diego].)
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The above figure is
reproduced from the cited reference
with permission from Cell Press
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Secondary reference #3
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Title
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The structure of calcyclin reveals a novel homodimeric fold for s100 ca(2+)-Binding proteins.
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Authors
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B.C.Potts,
J.Smith,
M.Akke,
T.J.Macke,
K.Okazaki,
H.Hidaka,
D.A.Case,
W.J.Chazin.
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Ref.
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Nat Struct Biol, 1995,
2,
790-796.
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PubMed id
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