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G-protein activation by a metabotropic glutamate receptor. Seven AB, Barros-Álvarez X et al. Nature. 2021 Jul 15;595(7867):450-454.

Structure and dynamics of semaglutide- and taspoglutide-bound GLP-1R-Gs complexes. Zhang X, Belousoff MJ et al. Cell Rep. 2021 Jul 13;36(2):109374.

Nuclear cGAS: guard or prisoner? de Oliveira Mann CC, Hopfner KP. EMBO J. 2021 Jul 12:e108293.

Nanobodies from camelid mice and llamas neutralize SARS-CoV-2 variants. Xu J, Xu K et al. Nature. 2021 Jul 8;595(7866):278-282.

Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity. Gupta TK, Klumpe S et al. Cell. 2021 Jul 8;184(14):3643-3659.e23.

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News

May 28, 2021

The ChimeraX 1.2 production release is available. See the change log for what's new.

May 6, 2021

We're looking for somebody to join the ChimeraX development team! Please see the job posting for details.

December 11, 2020

The RBVI wishes you a safe and happy holiday season! See our 2020 card and the gallery of previous cards back to 1985.

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UCSF ChimeraX

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.

Feature Highlight

membrane protein with lipophilicity coloring

Coloring by Molecular Lipophilicity Potential

Molecular lipophilicity potential (MLP) can be calculated for a protein and displayed with surface coloring using the command mlp or the Molecule Display icon . The image shows the photosynthetic reaction center from a purple sulfur bacterium, with MLP coloring on the molecular surface and membrane boundaries from OPM (Orientations of Proteins in Membranes entry 1eys). Blue and red balls represent the cytoplasmic and periplasmic sides of the bacterial inner membrane, respectively. Parts of the L, M, and H chains span the membrane, whereas the cytochrome subunit sits on the periplasmic side, at the top. The surface coloring ranges from dark goldenrod for the most hydrophobic potentials, through white, to dark cyan for the most hydrophilic. Ligands including lipid, detergent, heme, and various other cofactors are shown as purple surfaces.

For image setup after the structure from OPM has been opened, see the command file mlp.cxc.

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Example Image

transducin switch regions

G-Protein Switch Regions

The GDP- and GTP-bound conformations of the transducin α-subunit (1tag and 1tnd, respectively) differ primarily in three regions, termed switch 1, switch 2, and switch 3. The structures have been superimposed with matchmaker and shown as cartoons, with “empty” outlines where the structures are almost the same (for simplicity, only one conformation's outlines are shown). The GTP analog GTPγS is displayed as spheres color-coded by heteroatom. For 2D labels and image setup other than structure orientation, see the command file switch.cxc.

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