ArticleProceedings of the National Academy of Sciences of the United States of America2009
Inherent flexibility determines the transition mechanisms of the EF-hands of calmodulin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed.
- A Hydrophobic Cluster Modulates Long-Range Allostery in the TRMT2A RNA Recognition Motif.Journal of chemical information and modeling · 2026Article
- Role of water-bridged interactions in metal ion coupled protein allostery.PLoS computational biology · 2022Article
- The mechanism of complex formation between calmodulin and voltage gated calcium channels revealed by molecular dynamics.PloS one · 2021Article
- Uncovering the Early Stages of Domain Melting in Calmodulin with Ultrafast Temperature-Jump Infrared Spectroscopy.The journal of physical chemistry. B · 2019Article
- Molecular mechanism of multispecific recognition of Calmodulin through conformational changes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Interaction with adenylate cyclase toxin fromFEBS open bio · 2017Article
- Conformational heterogeneity of the calmodulin binding interface.Nature communications · 2016Article
- Lessons in Protein Design from Combined Evolution and Conformational Dynamics.Scientific reports · 2015Article
- Conformational frustration in calmodulin-target recognition.Journal of molecular recognition : JMR · 2015Article
- Insights into the species-specific TLR4 signaling mechanism in response to Rhodobacter sphaeroides lipid A detection.Scientific reports · 2015Article
- Modulation of calmodulin lobes by different targets: an allosteric model with hemiconcerted conformational transitions.PLoS computational biology · 2015Article
- Distinguishing unfolding and functional conformational transitions of calmodulin using ultraviolet resonance Raman spectroscopy.Protein science : a publication of the Protein Society · 2014Article
- Energy landscape views for interplays among folding, binding, and allostery of calmodulin domains.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Protein recognition and selection through conformational and mutually induced fit.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Simulating movement of tRNA through the ribosome during hybrid-state formation.The Journal of chemical physics · 2013Article
- Mapping conformational dynamics of proteins using torsional dynamics simulations.Biophysical journal · 2013Article
- Disorder guides protein function.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Retention of conformational entropy upon calmodulin binding to target peptides is driven by transient salt bridges.Biophysical journal · 2012Article
- Protein flexibility is key to cisplatin crosslinking in calmodulin.Protein science : a publication of the Protein Society · 2012Article
- Biomolecular dynamics: order-disorder transitions and energy landscapes.Reports on progress in physics. Physical Society (Great Britain) · 2012Article
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2 authors.
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Abstract
We explore how inherent flexibility of a protein molecule influences the mechanism controlling allosteric transitions by using a variational model inspired from work in protein folding. The striking differences in the predicted transition mechanism for the opening of the two domains of calmodulin (CaM) emphasize that inherent flexibility is key to understanding the complex conformational changes that occur in proteins. In particular, the C-terminal domain of CaM (cCaM), which is inherently less flexible than its N-terminal domain (nCaM), reveals "cracking" or local partial unfolding during the open/closed transition. This result is in harmony with the picture that cracking relieves local stresses caused by conformational deformations of a sufficiently rigid protein. We also compare the conformational transition in a recently studied even-odd paired fragment of CaM. Our results rationalize the different relative binding affinities of the EF-hands in the engineered fragment compared with the intact odd-even paired EF-hands (nCaM and cCaM) in terms of changes in flexibility along the transition route. Aside from elucidating general theoretical ideas about the cracking mechanism, these studies also emphasize how the remarkable intrinsic plasticity of CaM underlies conformational dynamics essential for its diverse functions.
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