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PDBsum entry 1cff
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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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Nmr solution structure of a complex of calmodulin with a binding peptide of the ca2+ pump.
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Authors
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B.Elshorst,
M.Hennig,
H.Försterling,
A.Diener,
M.Maurer,
P.Schulte,
H.Schwalbe,
C.Griesinger,
J.Krebs,
H.Schmid,
T.Vorherr,
E.Carafoli.
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Ref.
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Biochemistry, 1999,
38,
12320-12332.
[DOI no: ]
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PubMed id
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Abstract
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The three-dimensional structure of the complex between calmodulin (CaM) and a
peptide corresponding to the N-terminal portion of the CaM-binding domain of the
plasma membrane calcium pump, the peptide C20W, has been solved by heteronuclear
three-dimensional nuclear magnetic resonance (NMR) spectroscopy. The structure
calculation is based on a total of 1808 intramolecular NOEs and 49
intermolecular NOEs between the peptide C20W and calmodulin from
heteronuclear-filtered NOESY spectra and a half-filtered experiment,
respectively. Chemical shift differences between free Ca(2+)-saturated CaM and
its complex with C20W as well as the structure calculation reveal that C20W
binds solely to the C-terminal half of CaM. In addition, comparison of the
methyl resonances of the nine assigned methionine residues of free
Ca(2+)-saturated CaM with those of the CaM/C20W complex revealed a significant
difference between the N-terminal and the C-terminal domain; i.e., resonances in
the N-terminal domain of the complex were much more similar to those reported
for free CaM in contrast to those in the C-terminal half which were
significantly different not only from the resonances of free CaM but also from
those reported for the CaM/M13 complex. As a consequence, the global structure
of the CaM/C20W complex is unusual, i.e., different from other peptide
calmodulin complexes, since we find no indication for a collapsed structure. The
fine modulation in the peptide protein interface shows a number of differences
to the CaM/M13 complex studied by Ikura et al. [Ikura, M., Clore, G. M.,
Gronenborn, A. M., Zhu, G., Klee, C. B., and Bax, A. (1992) Science 256,
632-638]. The unusual binding mode to only the C-terminal half of CaM is in
agreement with the biochemical observation that the calcium pump can be
activated by the C-terminal half of CaM alone [Guerini, D., Krebs, J., and
Carafoli, E. (1984) J. Biol. Chem. 259, 15172-15177].
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