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PDBsum entry 1ckk
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Calmodulin-peptide complex
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PDB id
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1ckk
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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 novel target recognition revealed by calmodulin in complex with ca2+-Calmodulin-Dependent kinase kinase.
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Authors
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M.Osawa,
H.Tokumitsu,
M.B.Swindells,
H.Kurihara,
M.Orita,
T.Shibanuma,
T.Furuya,
M.Ikura.
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Ref.
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Nat Struct Biol, 1999,
6,
819-824.
[DOI no: ]
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PubMed id
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Abstract
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The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue
peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent
protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this
complex, the CaMKK peptide forms a fold comprising an alpha-helix and a
hairpin-like loop whose C-terminus folds back on itself. The binding orientation
of this CaMKK peptide by the two CaM domains is opposite to that observed in all
other CaM-target complexes determined so far. The N- and C-terminal hydrophobic
pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide,
respectively. This 14-residue separation between two key hydrophobic groups is
also unique among previously determined CaM complexes. The present structure
represents a new and distinct class of Ca2+/CaM target recognition that may be
shared by other Ca2+/CaM-stimulated proteins.
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Figure 2.
Figure 2. a, Schematic drawing of interacting residues between
Ca ^2+ /CaM and CaMKK peptide. Residues in N-domain and
C-domain are colored in cyan and violet, respectively. Key
residues of the CaMKK peptide anchoring the hydrophobic pocket
in each domain, Trp 444 and Phe 459, are shown in green. b,
Portions of ^13 C/F[3]-filtered ^13 C/F[1]-edited HMQC-NOESY
spectrum ^24 showing intermolecular NOEs between CaM and the
CaMKK peptide. Stereo drawing of the key residues of CaMKK
peptide in the hydrophobic pocket of c, N-domain and
d,C−domain. esidues within 5 Å of the key residues, Trp
444 and Phe 459, are shown. N, O and S atoms are colored in
blue, red and yellow, respectively, while C atoms of N- and
C-domain of CaM and CaMKK are shown in cyan, violet and gray,
respectively. Diagrams (c) and (d) were generated using the
program MOLMOL^55.
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Figure 3.
Figure 3. Electrostatic potential surfaces of the CaM−target
peptide complexes. In the upper panels, the surface of Ca ^2+
/CaM is shown with the target peptide as an yellow tube. The
peptide surface is in the lower panels. The surface is colored
according to the local electrostatic potential, with blue and
red representing positive and negative potential, respectively.
Acidic and basic residues interacting with the target peptide
are labeled in red and blue, respectively. a, CaM−CaMKK; b,
CaM−MLCK^19, ^20; c, CaM−CaMKII^21. The domain linker of CaM
in the CaM−CaMKII complex was modeled in the Insight II, since
residues 74−83 are absent from the PDB file because of the
high flexibility of this region.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1999,
6,
819-824)
copyright 1999.
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