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Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins
Masatoshi Maki1, Yasuyuki Kitaura, Hirokazu Satoh
1Laboratory of Molecular and Cellular Regulation, Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Japan. mmaki@agr.nagoya-u.ac.jp
Biochimica Et Biophysica Acta
|November 26, 2002
Summary
Penta-EF-hand (PEF) proteins are calcium-binding proteins with conserved structural features. Their functions are increasingly understood through identified interacting proteins, particularly noncatalytic mammalian PEF proteins.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Penta-EF-hand (PEF) proteins are a family of calcium-binding proteins characterized by five repetitive EF-hand motifs.
- These proteins share structural similarities, including specific alpha-helices linking EF-hand domains and common features like dimerization, N-terminal domains, and calcium-dependent membrane translocation.
Purpose of the Study:
- To review the structural characteristics and classification of Penta-EF-hand (PEF) proteins.
- To highlight the emerging understanding of the functions of noncatalytic mammalian PEF proteins.
Main Methods:
- Comparative analysis of amino acid sequences to classify mammalian PEF proteins into Group I (e.g., ALG-2, peflin) and Group II (e.g., calpain subfamily, sorcin, grancalcin).
- Review of recent findings on specific interacting proteins associated with PEF proteins.
Main Results:
- Mammalian PEF proteins are classified into two main groups based on sequence homology.
- Group I PEF genes are conserved across diverse organisms, from lower animals to plants and fungi.
- Specific interacting proteins are beginning to elucidate the roles of noncatalytic mammalian PEF proteins.
Conclusions:
- Penta-EF-hand proteins represent a conserved family with distinct structural and functional characteristics.
- The study of PEF protein interactions is crucial for understanding their diverse biological roles, especially in noncatalytic mammalian proteins.