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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 391, Issue 10 (Oct 2010)

Issues

New structural aspects of FKBP38 activation

Mitcheell Maestre-Martínez
  • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
  • Present address: Max Planck Institute for Biophysical Chemistry, Am Faßberg 11, D-37077 Göttingen, Germany.
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Katja Haupt
  • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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  • De Gruyter OnlineGoogle Scholar
/ Frank Edlich
  • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
  • Present address: National Institute of Neurological Disorders and Stroke, NIH, 35 Convent Drive MSC 3704, Bethesda, MD 20892, USA.
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  • De Gruyter OnlineGoogle Scholar
/ Günther Jahreis
  • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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  • De Gruyter OnlineGoogle Scholar
/ Franziska Jarczowski
  • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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  • De Gruyter OnlineGoogle Scholar
/ Frank Erdmann
  • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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/ Gunter Fischer
  • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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/ Christian Lücke
  • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany
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Published Online: 2010-08-13 | DOI: https://doi.org/10.1515/bc.2010.122

Abstract

The human FK506-binding protein 38 (FKBP38) regulates Bcl-2 in neuronal apoptosis. To control Bcl-2 activity, FKBP38 requires a prior interaction with the Ca2+-sensor calmodulin (CaM). The resulting FKBP38/CaM complex is unique within the FKBP family. Here, we present novel insights into the structural arrangement of this complex. Chemical shift perturbation analyses of the individual protein domains revealed two separate interaction sites between FKBP38 and CaM. On the one hand, residues Glu303, Tyr307 and Leu311, belonging to the predicted CaM-binding site at the C-terminal end of FKBP38, become embedded in the hydrophobic target protein-binding cleft of the C-terminal CaM lobe. On the other hand, in a second binding interaction, the N-terminal end of the catalytic FKBP38 domain shows surface contacts to the AB and CD loops of CaM as well as the adjacent helices. Furthermore, a Glu-rich region at the non-structured FKBP38 N-terminus features additional contacts to CaM helix A. In combination with previous results, we thus conclude that the FKBP38/CaM complex is constituted by (i) a Ca2+-dependent interaction of the CaM-binding motif at the C-terminal end of FKBP38 with the C-terminal CaM lobe and (ii) a Ca2+-independent interaction between the N-terminal CaM lobe and the N-terminal region of the catalytic FKBP38 domain.

Keywords: Bcl-2; calmodulin; chemical shift perturbation mapping; FK506 binding protein; PPIase; protein-protein interactions

About the article

Corresponding author


Received: 2010-03-25

Accepted: 2010-07-05

Published Online: 2010-08-13

Published in Print: 2010-10-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.122.

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