1cff

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[[Image:1cff.gif|left|200px]]
[[Image:1cff.gif|left|200px]]
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{{Structure
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|PDB= 1cff |SIZE=350|CAPTION= <scene name='initialview01'>1cff</scene>
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The line below this paragraph, containing "STRUCTURE_1cff", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span>
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{{STRUCTURE_1cff| PDB=1cff | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cff OCA], [http://www.ebi.ac.uk/pdbsum/1cff PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cff RCSB]</span>
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'''NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING PEPTIDE OF THE CA2+-PUMP'''
'''NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING PEPTIDE OF THE CA2+-PUMP'''
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[[Category: Schwalbe, H.]]
[[Category: Schwalbe, H.]]
[[Category: Vorherr, T.]]
[[Category: Vorherr, T.]]
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[[Category: c20w]]
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[[Category: C20w]]
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[[Category: calmodulin]]
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[[Category: Calmodulin]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: plasma membrane calcium pump]]
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[[Category: Plasma membrane calcium pump]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:40:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:20:38 2008''
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Revision as of 09:40, 2 May 2008

Image:1cff.gif

Template:STRUCTURE 1cff

NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING PEPTIDE OF THE CA2+-PUMP


Overview

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].

About this Structure

1CFF is a Protein complex structure of sequences from Homo sapiens and Xenopus laevis. Full crystallographic information is available from OCA.

Reference

NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump., Elshorst B, Hennig M, Forsterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E, Biochemistry. 1999 Sep 21;38(38):12320-32. PMID:10493800 Page seeded by OCA on Fri May 2 12:40:35 2008

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