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Fluorescent indicators for Ca2+based on green fluorescent proteins and calmodulin
New fluorescent indicators for Ca2+ that are genetically encoded without cofactors and are targetable to specific intracellular locations are constructed and dubbed ‘cameleons’.
Calmodulin Target Database
- K. Yap, Justin Kim, K. Truong, Marc S. Sherman, T. Yuan, M. Ikura
- BiologyJournal of Structural and Functional Genomics
A web-based database is developed that can predict a putative CRS location within a given protein sequence, identify the subclass to which it may belong, and structural and biophysical parameters such as hydrophobicity, hydrophobic moment, and propensity for a -helix formation.
Solution structure of a calmodulin-target peptide complex by multidimensional NMR.
The three-dimensional solution structure of the complex between calcium-bound calmodulin (Ca(2+)-CaM) and a 26-residue synthetic peptide comprising the CaM binding domain (residues 577 to 602) of…
Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
- Mingjie Zhang, Toshiyuki Tanaka, M. Ikura
- Chemistry, BiologyNature Structural Biology
- 1 September 1995
The solution structure of Ca2-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca2+-saturated form, and concerted movements of helices A and D with respect to B and C, are likely responsible for the cooperative Ca2+,binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains.
Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible.
The backbone dynamics of Ca(2+)-saturated recombinant Drosophila calmodulin has been studied by 15N longitudinal and transverse relaxation experiments, combined with 15N(1H) NOE measurements, showing a high degree of mobility near the middle of the central helix and anisotropy observed in the motion of the two globular cal modulin domains is much smaller than expected.
Molecular and structural basis of target recognition by calmodulin.
The structural aspects of target recognition by Ca(2+)-CaM are discussed using mainly the three-dimensional structural information obtained with nuclear magnetic resonance spectroscopy and X-ray diffraction methods.
Structural basis of calcium-induced E-cadherin rigidification and dimerization
The E-cadherin dual-domain structure reported here defines the role played by calcium in the cadherin-mediated formation and maintenance of solid tissues.
MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli.