Intracellular Calcium-Binding Proteins in Signal Transduction
Cell stimulation generates a Ca2+ signal, which is perceived by intracellular Ca2+-binding proteins. These proteins are made up of different units of a conserved structural motif, called the 2S domain, and composed mainly of four ?-helices and two anti parallel ?-strands. This 2S domain ca...
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| Format: | Article |
| Language: | deu |
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Swiss Chemical Society
1992-04-01
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| Series: | CHIMIA |
| Online Access: | https://chimia.ch/chimia/article/view/2120 |
| _version_ | 1819280003691446272 |
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| author | Jos A. Cox |
| author_facet | Jos A. Cox |
| author_sort | Jos A. Cox |
| collection | DOAJ |
| description |
Cell stimulation generates a Ca2+ signal, which is perceived by intracellular Ca2+-binding proteins. These proteins are made up of different units of a conserved structural motif, called the 2S domain, and composed mainly of four ?-helices and two anti
parallel ?-strands. This 2S domain can bind 2 Ca2+ ions and is roughly cup-shaped in the Ca2+-bound configuration. The interior of the cup is lined with solvent-exposed hydrophobic residues. In Ca2+-binding proteins involved in cellular signal-response
coupling, such as calmodulin and troponin C, the hydrophobic cup is essential for interaction with, and activation of the response proteins. The Ca2+-free state is characterized by a reorientation of the ?-helices and shielding of the hydrophobic residues in the cup.
In contrast, interaction with the target strongly stabilizes the hydrophobic cups. Ca2+-buffering proteins, such as parvalbumin and sarcoplasmic Ca2+-binding proteins, have intrinsically a stable conformation, since the strongly hydrophobic cups are stabilized by frontal
self association of the 2S domains.
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| first_indexed | 2024-12-24T00:36:53Z |
| format | Article |
| id | doaj.art-1526b8dc2d0745c99e803533a184bc64 |
| institution | Directory Open Access Journal |
| issn | 0009-4293 2673-2424 |
| language | deu |
| last_indexed | 2024-12-24T00:36:53Z |
| publishDate | 1992-04-01 |
| publisher | Swiss Chemical Society |
| record_format | Article |
| series | CHIMIA |
| spelling | doaj.art-1526b8dc2d0745c99e803533a184bc642022-12-21T17:24:04ZdeuSwiss Chemical SocietyCHIMIA0009-42932673-24241992-04-01464Intracellular Calcium-Binding Proteins in Signal TransductionJos A. Cox Cell stimulation generates a Ca2+ signal, which is perceived by intracellular Ca2+-binding proteins. These proteins are made up of different units of a conserved structural motif, called the 2S domain, and composed mainly of four ?-helices and two anti parallel ?-strands. This 2S domain can bind 2 Ca2+ ions and is roughly cup-shaped in the Ca2+-bound configuration. The interior of the cup is lined with solvent-exposed hydrophobic residues. In Ca2+-binding proteins involved in cellular signal-response coupling, such as calmodulin and troponin C, the hydrophobic cup is essential for interaction with, and activation of the response proteins. The Ca2+-free state is characterized by a reorientation of the ?-helices and shielding of the hydrophobic residues in the cup. In contrast, interaction with the target strongly stabilizes the hydrophobic cups. Ca2+-buffering proteins, such as parvalbumin and sarcoplasmic Ca2+-binding proteins, have intrinsically a stable conformation, since the strongly hydrophobic cups are stabilized by frontal self association of the 2S domains. https://chimia.ch/chimia/article/view/2120 |
| spellingShingle | Jos A. Cox Intracellular Calcium-Binding Proteins in Signal Transduction CHIMIA |
| title | Intracellular Calcium-Binding Proteins in Signal Transduction |
| title_full | Intracellular Calcium-Binding Proteins in Signal Transduction |
| title_fullStr | Intracellular Calcium-Binding Proteins in Signal Transduction |
| title_full_unstemmed | Intracellular Calcium-Binding Proteins in Signal Transduction |
| title_short | Intracellular Calcium-Binding Proteins in Signal Transduction |
| title_sort | intracellular calcium binding proteins in signal transduction |
| url | https://chimia.ch/chimia/article/view/2120 |
| work_keys_str_mv | AT josacox intracellularcalciumbindingproteinsinsignaltransduction |