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Relating form and function of EF-hand calcium binding proteins.

Walter J Chazin1

  • 1Department of Biochemistry and Chemistry, Vanderbilt University, Nashville, Tennessee 37232-8725, USA. walter.chazin@vanderbilt.edu

Accounts of Chemical Research
|February 15, 2011
PubMed
Summary

EF-hand calcium-binding proteins (EFCaBPs) are crucial for cellular signaling. Our research clarifies how their sequences dictate function and target interactions, advancing understanding for medicine and biotechnology.

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Area of Science:

  • Structural biology and biochemistry
  • Molecular mechanisms of protein function
  • Calcium signaling pathways

Background:

  • EF-hand motifs are common in animal genomes, forming EF-hand calcium-binding proteins (EFCaBPs) distributed throughout cells.
  • Current understanding lacks insight into how peptide sequences determine EFCaBP functions and target specificity.
  • Elucidating these mechanisms is vital for understanding EFCaBP roles in health and disease, and for medical/biotechnological applications.

Purpose of the Study:

  • To investigate the sequence-to-function relationship in EFCaBPs through structural and biochemical approaches.
  • To define the conformational changes induced by calcium binding in EFCaBPs.
  • To elucidate the molecular mechanisms underlying EFCaBP target recognition and signal transduction.

Main Methods:

  • Solution NMR spectroscopy to determine protein structures and conformational changes.
  • Site-directed mutagenesis and protein engineering to identify critical residues.
  • Biochemical assays to study protein-ligand interactions and cooperativity.

Main Results:

  • Identified key residues differentiating calcium response in homologous EFCaBPs like calbindin D(9k) and calmodulin (CaM).
  • Established cooperativity in calcium ion binding as a mechanism for detecting small concentration changes.
  • Characterized the dimeric architecture of S100 proteins and their target interactions, and revealed novel binding characteristics of centrin.

Conclusions:

  • Subtle sequence variations fine-tune EFCaBPs for specific target interactions.
  • Developed a dual-molecular-switch model for CaM and EF-hand domain roles in regulating ion channel gating.
  • Discovered extracellular functions of EFCaBPs, including the antimicrobial activity of S100A8/S100A9, and their interactions with cell surface receptors.