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PDBsum entry 1lin
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Calcium-binding protein
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PDB id
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1lin
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Contents |
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* Residue conservation analysis
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Nat Struct Biol
1:795-801
(1994)
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PubMed id:
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Trifluoperazine-induced conformational change in Ca(2+)-calmodulin.
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M.Vandonselaar,
R.A.Hickie,
J.W.Quail,
L.T.Delbaere.
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ABSTRACT
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Here we show that, as a consequence of binding the drug trifluoperazine, a major
conformational movement occurs in Ca(2+)-calmodulin (CaM). The tertiary
structure changes from an elongated dumb-bell, with exposed hydrophobic
surfaces, to a compact globular form which can no longer interact with its
target enzymes. It is likely that inactivation of Ca(2+)-CaM by trifluoperazine
is due to this major tertiary-structural alteration in Ca(2+)-CaM, which is
initiated and stabilized by drug binding. This conformational change is similar
to that which occurs on the binding of Ca(2+)-CaM to target peptides. Two
hydrophobic binding pockets, created by amino acid residues adjacent to
Ca(2+)-coordinating residues, form the key recognition sites on Ca(2+)-CaM for
both inhibitors and target enzymes.
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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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A.Reyes-Ramírez,
M.Leyte-Lugo,
M.Figueroa,
T.Serrano-Alba,
M.González-Andrade,
and
R.Mata
(2011).
Synthesis, biological evaluation, and docking studies of gigantol analogs as calmodulin inhibitors.
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Eur J Med Chem,
46,
2699-2708.
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F.Erdmann,
N.Schäuble,
S.Lang,
M.Jung,
A.Honigmann,
M.Ahmad,
J.Dudek,
J.Benedix,
A.Harsman,
A.Kopp,
V.Helms,
A.Cavalié,
R.Wagner,
and
R.Zimmermann
(2011).
Interaction of calmodulin with Sec61α limits Ca2+ leakage from the endoplasmic reticulum.
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EMBO J,
30,
17-31.
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A.Ahmed,
S.Villinger,
and
H.Gohlke
(2010).
Large-scale comparison of protein essential dynamics from molecular dynamics simulations and coarse-grained normal mode analyses.
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Proteins,
78,
3341-3352.
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J.A.Bartos,
J.D.Ulrich,
H.Li,
M.A.Beazely,
Y.Chen,
J.F.Macdonald,
and
J.W.Hell
(2010).
Postsynaptic clustering and activation of Pyk2 by PSD-95.
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J Neurosci,
30,
449-463.
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M.D.Feldkamp,
S.E.O'Donnell,
L.Yu,
and
M.A.Shea
(2010).
Allosteric effects of the antipsychotic drug trifluoperazine on the energetics of calcium binding by calmodulin.
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Proteins,
78,
2265-2282.
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V.N.Malashkevich,
N.G.Dulyaninova,
U.A.Ramagopal,
M.A.Liriano,
K.M.Varney,
D.Knight,
M.Brenowitz,
D.J.Weber,
S.C.Almo,
and
A.R.Bresnick
(2010).
Phenothiazines inhibit S100A4 function by inducing protein oligomerization.
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Proc Natl Acad Sci U S A,
107,
8605-8610.
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PDB code:
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J.Qin,
A.V.Zima,
M.Porta,
L.A.Blatter,
and
M.Fill
(2009).
Trifluoperazine: a rynodine receptor agonist.
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Pflugers Arch,
458,
643-651.
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S.L.Shirran,
and
P.E.Barran
(2009).
The use of ESI-MS to probe the binding of divalent cations to calmodulin.
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J Am Soc Mass Spectrom,
20,
1159-1171.
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S.L.Russell,
N.V.McFerran,
E.M.Hoey,
A.Trudgett,
and
D.J.Timson
(2007).
Characterisation of two calmodulin-like proteins from the liver fluke, Fasciola hepatica.
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Biol Chem,
388,
593-599.
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K.Chen,
J.Ruan,
and
L.A.Kurgan
(2006).
Prediction of three dimensional structure of calmodulin.
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Protein J,
25,
57-70.
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L.Milanesi,
C.A.Hunter,
S.E.Sedelnikova,
and
J.P.Waltho
(2006).
Amplification of bifunctional ligands for calmodulin from a dynamic combinatorial library.
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Chemistry,
12,
1081-1087.
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P.Petrone,
and
V.S.Pande
(2006).
Can conformational change be described by only a few normal modes?
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Biophys J,
90,
1583-1593.
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T.Kaneko,
C.Harasztosi,
A.F.Mack,
and
A.W.Gummer
(2006).
Membrane traffic in outer hair cells of the adult mammalian cochlea.
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Eur J Neurosci,
23,
2712-2722.
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I.Horváth,
V.Harmat,
A.Perczel,
V.Pálfi,
L.Nyitray,
A.Nagy,
E.Hlavanda,
G.Náray-Szabó,
and
J.Ovádi
(2005).
The structure of the complex of calmodulin with KAR-2: a novel mode of binding explains the unique pharmacology of the drug.
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J Biol Chem,
280,
8266-8274.
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PDB code:
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S.J.Watt,
A.Oakley,
M.M.Sheil,
and
J.L.Beck
(2005).
Comparison of negative and positive ion electrospray ionization mass spectra of calmodulin and its complex with trifluoperazine.
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Rapid Commun Mass Spectrom,
19,
2123-2130.
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A.G.Turjanski,
D.A.Estrin,
R.E.Rosenstein,
J.E.McCormick,
S.R.Martin,
A.Pastore,
R.R.Biekofsky,
and
V.Martorana
(2004).
NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
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Protein Sci,
13,
2925-2938.
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C.M.Shepherd,
and
H.J.Vogel
(2004).
A molecular dynamics study of Ca(2+)-calmodulin: evidence of interdomain coupling and structural collapse on the nanosecond timescale.
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Biophys J,
87,
780-791.
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D.B.Sherman,
S.Zhang,
J.B.Pitner,
and
A.Tropsha
(2004).
Evaluation of the relative stability of liganded versus ligand-free protein conformations using Simplicial Neighborhood Analysis of Protein Packing (SNAPP) method.
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Proteins,
56,
828-838.
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J.S.Shim,
J.Lee,
H.J.Park,
S.J.Park,
and
H.J.Kwon
(2004).
A new curcumin derivative, HBC, interferes with the cell cycle progression of colon cancer cells via antagonization of the Ca2+/calmodulin function.
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Chem Biol,
11,
1455-1463.
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M.Matsubara,
T.Nakatsu,
H.Kato,
and
H.Taniguchi
(2004).
Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulin.
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EMBO J,
23,
712-718.
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PDB code:
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S.N.Reuland,
A.P.Vlasov,
and
S.A.Krupenko
(2003).
Disruption of a calmodulin central helix-like region of 10-formyltetrahydrofolate dehydrogenase impairs its dehydrogenase activity by uncoupling the functional domains.
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J Biol Chem,
278,
22894-22900.
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S.W.Vetter,
and
E.Leclerc
(2003).
Novel aspects of calmodulin target recognition and activation.
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Eur J Biochem,
270,
404-414.
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H.H.Gan,
R.A.Perlow,
S.Roy,
J.Ko,
M.Wu,
J.Huang,
S.Yan,
A.Nicoletta,
J.Vafai,
D.Sun,
L.Wang,
J.E.Noah,
S.Pasquali,
and
T.Schlick
(2002).
Analysis of protein sequence/structure similarity relationships.
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Biophys J,
83,
2781-2791.
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M.L.Mattinen,
K.Pääkkönen,
T.Ikonen,
J.Craven,
T.Drakenberg,
R.Serimaa,
J.Waltho,
and
A.Annila
(2002).
Quaternary structure built from subunits combining NMR and small-angle x-ray scattering data.
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Biophys J,
83,
1177-1183.
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H.Patel,
S.S.Margossian,
and
P.D.Chantler
(2000).
Locking regulatory myosin in the off-state with trifluoperazine.
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J Biol Chem,
275,
4880-4888.
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S.Y.Lee,
and
R.E.Klevit
(2000).
The whole is not the simple sum of its parts in calmodulin from S. cerevisiae.
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Biochemistry,
39,
4225-4230.
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Y.Li,
M.L.Love,
J.A.Putkey,
and
C.Cohen
(2000).
Bepridil opens the regulatory N-terminal lobe of cardiac troponin C.
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Proc Natl Acad Sci U S A,
97,
5140-5145.
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PDB code:
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Z.Li,
S.H.Kim,
J.M.Higgins,
M.B.Brenner,
and
D.B.Sacks
(1999).
IQGAP1 and calmodulin modulate E-cadherin function.
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J Biol Chem,
274,
37885-37892.
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B.G.Vertessy,
V.Harmat,
Z.Böcskei,
G.Náray-Szabó,
F.Orosz,
and
J.Ovádi
(1998).
Simultaneous binding of drugs with different chemical structures to Ca2+-calmodulin: crystallographic and spectroscopic studies.
|
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Biochemistry,
37,
15300-15310.
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PDB code:
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W.Shen,
and
M.M.Slaughter
(1998).
Metabotropic and ionotropic glutamate receptors regulate calcium channel currents in salamander retinal ganglion cells.
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J Physiol,
510,
815-828.
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J.P.Williams,
J.M.McDonald,
M.A.McKenna,
S.E.Jordan,
W.Radding,
and
H.C.Blair
(1997).
Differential effects of tamoxifen-like compounds on osteoclastic bone degradation, H(+)-ATPase activity, calmodulin-dependent cyclic nucleotide phosphodiesterase activity, and calmodulin binding.
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J Cell Biochem,
66,
358-369.
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C.J.Craven,
B.Whitehead,
S.K.Jones,
E.Thulin,
G.M.Blackburn,
and
J.P.Waltho
(1996).
Complexes formed between calmodulin and the antagonists J-8 and TFP in solution.
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Biochemistry,
35,
10287-10299.
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H.H.Pierce,
N.Adey,
and
B.K.Kay
(1996).
Identification of cyclized calmodulin antagonists from a phage display random peptide library.
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Mol Divers,
1,
259-265.
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M.A.Kutuzov,
and
N.Bennett
(1996).
Calcium-activated opsin phosphatase activity in retinal rod outer segments.
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Eur J Biochem,
238,
613-622.
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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
code is
shown on the right.
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Links
