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Related Experiment Videos

The C2 domain calcium-binding motif: structural and functional diversity

E A Nalefski1, J J Falke

  • 1Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215, USA.

Protein Science : a Publication of the Protein Society
|December 1, 1996
PubMed
Summary

The C2 domain, a calcium-binding motif, is crucial for cellular signaling and membrane interactions. This review aligns 65 C2 domains, revealing two distinct structural folds and key residues for function.

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C2 domains from different Ca2+ signaling pathways display functional and mechanistic diversity.

Biochemistry·2001

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Structural Biology

Background:

  • The C2 domain is a conserved calcium (Ca2+)-binding motif found in numerous eukaryotic signaling proteins.
  • These domains are involved in critical cellular processes such as membrane trafficking, lipid signaling, GTPase activation, and protein phosphorylation.
  • C2 domains exhibit diverse ligand-binding capabilities, including Ca2+, phospholipids, and proteins, though not all are Ca2+-regulated.

Purpose of the Study:

  • To review the current understanding of C2 domain structure and function.
  • To present a novel sequence alignment of 65 C2 domain primary structures.
  • To predict the structural folds and identify critical residues for Ca2+ binding and regulation.

Main Methods:

  • Sequence alignment of 65 C2 domain primary structures.

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  • Analysis of existing crystal structures (e.g., synaptotagmin 1, phospholipase C-delta 1).
  • Comparative analysis to predict structural folds and functional residues.

    • Main Results:

    • The sequence alignment predicts two distinct topological folds for C2 domains.
    • Key residues potentially involved in the C2 domain fold and Ca2+ binding are highlighted.
    • Structural information from synaptotagmin 1 and phospholipase C-delta 1 supports the predicted folds.

    Conclusions:

    • C2 domains possess diverse structures and functions, with some potentially lacking Ca2+ regulation.
    • The identified structural folds provide a framework for understanding C2 domain mechanisms.
    • Further research can focus on the highlighted residues to elucidate specific C2 domain roles in cellular signaling.