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Backbone Dynamics of a Symmetric Calmodulin Dimer in Complex with the Calmodulin-Binding Domain of the Basic-Helix-Loop-Helix Transcription Factor SEF2-1/E2-2: A Highly Dynamic Complex
Calmodulin (CaM) interacts specifically as a dimer with some dimeric basic-Helix-Loop-Helix (bHLH) transcription factors via a novel high affinity binding mode. Here we report a study of the backbone dynamics by (15)N-spin relaxation on the CaM dimer in complex with a dimeric peptide that mimics the...
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| Hoofdauteurs: | , , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Biophysical Society
2005
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1366606/ https://ncbi.nlm.nih.gov/pubmed/15894636 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.104.055780 |
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