Structural diversity of calmodulin binding to its target sites
Henning Tidow,Poul Nissen +1 more
TLDR
This minireview analyzes the large number of CaM‐complex structures deposited in the Protein Data Bank to gain insight into the structural diversity ofCaM‐binding sites and mechanisms, such as those for Ca M‐activated protein kinases and phosphatases, voltage‐gated Ca2+‐channels and the plasma membrane Ca2‐ATPase.Abstract:
Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM-complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM-binding sites and mechanisms, such as those for CaM-activated protein kinases and phosphatases, voltage-gated Ca(2+)-channels and the plasma membrane Ca(2+)-ATPase.read more
Citations
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Short linear motifs: ubiquitous and functionally diverse protein interaction modules directing cell regulation.
Kim Van Roey,Bora Uyar,Robert J. Weatheritt,Holger Dinkel,Markus Seiler,Aidan Budd,Toby J. Gibson,Norman E. Davey,Norman E. Davey +8 more
TL;DR: Interaction Modules Directing Cell Regulation Kim Van Roey, Bora Uyar,† Robert J. Weatheritt,‡ Holger Dinkel,† Markus Seiler,† Aidan Budd,† Toby J. Gibson,† and Norman E. Davey*.
Journal ArticleDOI
Targeting Aquaporin-4 Subcellular Localization to Treat Central Nervous System Edema
Philip Kitchen,Mootaz M. Salman,Mootaz M. Salman,Mootaz M. Salman,Andrea M. Halsey,Charlotte Clarke-Bland,Justin A. MacDonald,Hiroaki Ishida,Hans J. Vogel,Sharif Almutiri,Sharif Almutiri,Ann Logan,Stefan Kreida,Tamim Al-Jubair,Julie Winkel Missel,Pontus Gourdon,Pontus Gourdon,Susanna Törnroth-Horsefield,Matthew T. Conner,Zubair Ahmed,Alex C. Conner,Roslyn M. Bill +21 more
TL;DR: It is shown that AQP4 cell-surface abundance increases in response to hypoxia-induced cell swelling in a calmodulin-dependent manner, and it is proposed that targeting the mechanism of cal modulin-mediated cell- surface localization of AQP 4 is a viable strategy for development of CNS edema therapies.
Journal ArticleDOI
Structural and Mechanistic Insights into Protein Translocation.
TL;DR: Structural data and biochemical experiments have elucidated how channel partners, the ribosome in cotranslational translocation, and the eukaryotic ER chaperone BiP or the prokaryotic cytosolic SecA ATPase in posttranslated translocation move polypeptides unidirectionally across the membrane.
Journal ArticleDOI
Physical characterization of nanoparticle size and surface modification using particle scattering diffusometry
TL;DR: Particle Scattering Diffusometry is presented, a method that utilizes dark field microscopy and the principles of particle image velocimetry to measure the diffusivity of particles undergoing Brownian motion and can reliably aid in a wide variety of applications, including colloid sizing, particle corona characterization, protein footprinting, and quantifying biomolecule activity.
Journal ArticleDOI
Activation mechanism of a human SK-calmodulin channel complex elucidated by cryo-EM structures.
TL;DR: Cryo–electron microscopy structures of a human SK4-CaM channel complex in closed and activated states reveal the gating mechanism of SK channels and provide a basis for understanding SK channel pharmacology.
References
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David Chin,Anthony R. Means +1 more
TL;DR: The calmodulin-dependent regulation of protein kinases illustrates the potential mechanisms by which Ca2+-sensing proteins can recognize and generate affinity and specificity for effectors in a Ca2-dependent manner.
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Solution structure of a calmodulin-target peptide complex by multidimensional NMR.
TL;DR: In this article, 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 skeletal muscle myosin light chain kinase, has been determined using multidimensional heteronuclear filtered and separated nuclear magnetic resonance spectroscopy.
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Structure of calmodulin refined at 2.2 A resolution.
TL;DR: The crystal structure of mammalian calmodulin has been refined at 2.2 A (1 A = 0.1 nm) resolution using a restrained least-squares method and shows a large hydrophobic cleft in each half of the molecule.
Journal ArticleDOI
Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex
TL;DR: The crystal structure of calcium-bound calmodulin bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined to a resolution of 2.4 angstroms.