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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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Detalhes bibliográficos
Main Authors: Larsson, Göran, Schleucher, Jürgen, Onions, Jacqueline, Hermann, Stefan, Grundström, Thomas, Wijmenga, Sybren S.
Formato: Artigo
Idioma:Inglês
Publicado em: Biophysical Society 2005
Assuntos:
Acesso em linha: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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