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Calmodulin-binding domains: just two faced or multi-faceted?
The Ca 2+-binding protein calmodulin binds to and activates several cellular enzymes in response to a rise in Ca 2+ concentration. It binds certain basic amphiphilic helices within these enzymes, which also act as autoinhibitory domains. The modulation of the binding equilibrium of these helices bet...
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Published in: | Trends in Biochemical Sciences 1995, Vol.20 (1), p.38-42 |
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container_end_page | 42 |
container_issue | 1 |
container_start_page | 38 |
container_title | Trends in Biochemical Sciences |
container_volume | 20 |
creator | James, Peter Vorherr, Thomas Carafoli, Ernesto |
description | The Ca
2+-binding protein calmodulin binds to and activates several cellular enzymes in response to a rise in Ca
2+ concentration. It binds certain basic amphiphilic helices within these enzymes, which also act as autoinhibitory domains. The modulation of the binding equilibrium of these helices between intramolecular (inhibition) and intermolecular (activation) sites forms a focal point for crosstalk between various signalling pathways. |
doi_str_mv | 10.1016/S0968-0004(00)88949-5 |
format | article |
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subjects | Amino Acid Sequence Animals Calmodulin-Binding Proteins - chemistry Calmodulin-Binding Proteins - physiology Models, Molecular Molecular Sequence Data Protein Structure, Tertiary Structure-Activity Relationship |
title | Calmodulin-binding domains: just two faced or multi-faceted? |
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