On the calcium-binding ability of the synthetic evolutionary ancestor of calcium-binding proteins
| Autor: | Yu. V. Mitin, E.E. Maximov, N.P. Zapevalova |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Genetics
chemistry.chemical_classification Parvalbumins Biophysics chemistry.chemical_element Peptide Cell Biology Calcium Biological Evolution Biochemistry Peptide Fragments Homology (biology) Troponin C chemistry Structural Biology Calcium-binding protein Gene duplication Amino Acid Sequence Carrier Proteins Molecular Biology Peptide sequence |
| Zdroj: | FEBS Letters. 88:80-82 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(78)80611-5 |
| Popis: | A number of calcium-binding proteins have a domain structure and the domain primary structures are rather similar. Parvalbumins have three domains, two of them are able to bind calcium [l] . Homology of this kind can be found in troponin C [2] and myosin alkali light chains [3] having four domains. Similarity of the primary and spatial structures of calcium-binding proteins and their domains suggested that there was a common evolutionary ancestor of these proteins and that subsequently gene duplication took place [4]. The ancestor structure was predicted [5] to be a 40-membered peptide with the following amino acid sequence |
| Databáze: | OpenAIRE |
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