Calcium Binding Dramatically Stabilizes an Ancestral Crystallin Fold in Tunicate βγ-Crystallin
| Autor: | Natalia Kozlyuk, Suvrajit Sengupta, Rachel W. Martin, Jan C. Bierma |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Conformation Sequence Homology Medical Biochemistry and Metabolomics Biochemistry Lens Protein structure Models Peptide sequence chemistry.chemical_classification biology Circular Dichroism Anatomy beta-Crystallins Ciona intestinalis Cell biology Tunicate Amino acid Amino Acid Protein stabilization Biochemistry & Molecular Biology Evolution Fluorescence Article Evolution Molecular Medicinal and Biomolecular Chemistry 03 medical and health sciences Crystallin Lens Crystalline Animals Humans Amino Acid Sequence gamma-Crystallins Binding site Eye Disease and Disorders of Vision Binding Sites Crystalline Sequence Homology Amino Acid 030102 biochemistry & molecular biology Spectrometry Molecular biology.organism_classification eye diseases Spectrometry Fluorescence 030104 developmental biology chemistry Calcium Biochemistry and Cell Biology sense organs |
| Zdroj: | Biochemistry, vol 55, iss 50 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | The tunicate (Ciona intestinalis) βγ-crystallin represents an intermediate case between the calcium-binding proteins ancestral to the vertebrate βγ-crystallin fold and the vertebrate structural crystallins. Unlike the structural βγ-crystallins in the vertebrate eye lens, this βγ-crystallin strongly binds Ca(2+). Furthermore, Ca(2+) binding greatly stabilizes the protein, an effect that has previously been observed in microbial βγ-crystallins but not in those of vertebrates. This relationship between binding and protein stabilization makes the tunicate βγ-crystallin an interesting model for studying the evolution of the human βγ-crystallin. We also compare and contrast the binding sites of tunicate βγ-crystallin with other βγ-crystallins in order to develop hypotheses as to the functional origin of the lack of the Ca(2+) binding sites in the human crystallins. |
| Databáze: | OpenAIRE |
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