Architecture and assembly mechanism of native glycine receptors. Zhu H, Gouaux E.. Nature. 2021 Nov 18;599(7885):513-517.
Target site selection and remodelling by type V CRISPR-transposon systems. Querques I, Schmitz M et al. Nature. 2021 Nov 18;599(7885):497-502.
The structure of neurofibromin isoform 2 reveals different functional states. Naschberger A, Baradaran R et al. Nature. 2021 Nov 11;599(7884):315-319.
Structural features of nucleosomes in interphase and metaphase chromosomes. Arimura Y, Shih RM et al. Mol Cell. 2021 Nov 4;81(21):4377-4397.e12.
Distinct allosteric mechanisms of first-generation MsbA inhibitors. Thélot FA, Zhang W et al. Science. 2021 Oct 29;374(6567):580-585.More citations...
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UCSF ChimeraX (or simply ChimeraX) is the next-generation molecular visualization program from the Resource for Biocomputing, Visualization, and Informatics (RBVI), following UCSF Chimera. ChimeraX can be downloaded free of charge for academic, government, nonprofit, and personal use. Commercial users, please see ChimeraX commercial licensing.
ChimeraX is developed with support from National Institutes of Health R01-GM129325 and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases.
AlphaFold is an artificial intelligence method for predicting protein structures. With the AlphaFold tool or command, ChimeraX can search for and load predicted structures from the freely available AlphaFold Database, automatically coloring them by confidence value:
The figure shows the predicted structure of UniProt entry TOM40_HUMAN, a channel protein needed to import other proteins into mitochondria. See the command file tom40.cxc for fetching data and other setup (background color, etc.).
Opening a sequence from UniProt also opens a dialog in which its annotations or “features” can be clicked to highlight those regions in both the sequence and the associated 3D structure. The low-confidence part of the structure (orange and red) maps to compositionally biased and likely disordered regions near the N-terminus of the sequence.More features...
KCNQ1 is the pore-forming subunit of a cardiac potassium channel. It binds to calmodulin, and mutations in either of these proteins can cause congenital long QT syndrome, a dangerous propensity for irregular heartbeats. In the image, a structure of the KCNQ1/calmodulin complex (PDB 5vms) has been assembled into the native tetrameric form with the sym command. The view is from the cytoplasmic side, with KCNQ1 shown as surfaces, calmodulin as cartoons, and calcium ions as balls. A pastel palette from ColorBrewer has been used to color the surfaces, darkened with color modify for the cartoons, and “rotated” 45° in hue for the ions. See the command file colormod.cxc.
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