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DNSN-1 recruits GINS for CMG helicase assembly during DNA replication initiation in Caenorhabditis elegans. Xia Y, Sonneville R et al. Science. 2023 Sep 22;381(6664):eadi4932.

Central role of Tim17 in mitochondrial presequence protein translocation. Fielden LF, Busch JD et al. Nature. 2023 Sep 21;621(7979):627–634.

Conserved class B GPCR activation by a biased intracellular agonist. Zhao LH, He Q et al. Nature. 2023 Sep 21;621(7979):635–641.

Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation. Juyoux P, Galdadas I et al. Science. 2023 Sep 15;381(6663):1217-1225.

Oligomerization-mediated activation of a short prokaryotic Argonaute. Shen Z, Yang XY et al. Nature. 2023 Sep 7;621(7977):154–161.

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News

May 9, 2023

The ChimeraX 1.6.1 production release is available! See the change log for what's new.

April 29, 2023

The ChimeraX 1.6 release candidate is available – please try it and report any issues. See the change log for what's new.

December 21, 2022

The RBVI wishes you a safe and happy holiday season! See our 2022 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, Chan Zuckerberg Initiative grant EOSS4-0000000439, and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases.

Feature Highlight

heterodimer modeling screenshot

Multichain Comparative Modeling

Modeller Comparative is an interface to Modeller for comparative (“homology”) modeling of proteins and protein complexes.

The example shows modeling the human (shades of blue) from the mouse (brown and tan) complex of programmed death-1 (PD-1) with its ligand PD-L2, PDB 3bp5.

Comparative modeling requires a template structure and a target-template sequence alignment for each unique chain. The sequences of human PD-1 and PD-L2 targets were fetched from UniProt and associated with the corresponding chains in the template structure, see model-pdl-setup.cxc. (Pairwise or multiple sequence alignments could have been used, but in this case, the template structure was simply associated with the target sequence.) Sequence-structure association shows mismatches in the Sequence Viewer: pink boxes for sequence differences between mouse and human, and gray outlines around the parts missing from the structure.

Three models were made with with default settings (other than the number of models), and the best-scoring model is shown. Two positions where sequence differences change the interfacial H-bonds are displayed.

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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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