Calcium-binding mechanism of human nonerythroid alpha-spectrin EF-structures

Biochemistry
S LundbergL Backman

Abstract

We have used circular dichroism and 1H- and 15N-NMR spectroscopy to investigate calcium binding to the two EF-hands of human nonerythroid or alphaII-spectrin. Comparison of the 1H-NMR spectra from the peptide containing both EF-hands to the peptides containing the single EF-I and EF-II structures showed that both the structural and calcium-binding properties are significantly different. Further studies of the 121 amino acid peptide containing both EF-hands using circular dichroism and NMR showed that the binding of calcium ions induces conformational changes. To investigate the calcium-binding mechanism, the chemical shifts changes were recorded using multidimensional NMR spectroscopy during calcium titration. A total of 25 titration curves were obtained, each corresponding to the chemical shift changes of individual amino acid residues. The shapes of these titration curves were either hyperbolic or sigmoidal. Using factor analysis, two functions were extracted, one hyperbolic and one sigmoidal, which accounted for nearly all information present in the titration curves. By fitting the two functions to binding curves based on different binding models, we found that the binding mechanism is best described as sequential. Since the...Continue Reading

References

Nov 1, 1992·Journal of Biomolecular NMR·M PiottoV Sklenár
Nov 13, 1990·European Journal of Biochemistry·D PietrobonT Pozzan
Jan 1, 1994·Methods in Enzymology·S Lundberg, L Backman
Jan 1, 1995·Methods in Enzymology·E I SolomonS Pulver
Jan 15, 1995·European Journal of Biochemistry·G TravéM Saraste
Feb 1, 1996·Current Opinion in Cell Biology·A Viel, D Branton

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Citations

Aug 31, 2011·Cellular and Molecular Life Sciences : CMLS·B MachnickaM C Lecomte
Jan 1, 1997·Annual Review of Physical Chemistry·R A GoldbeckD S Kliger
Feb 27, 2014·Cellular & Molecular Biology Letters·Dżamila M BogusławskaAleksander Czogalla

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