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Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism. Noddings CM, Wang RY et al. Nature. 2022 Jan 20;601(7893):465-469.

Cryo-EM structures of amyloid-β 42 filaments from human brains. Yang Y, Arseni D et al. Science. 2022 Jan 14;375(6577):167-172.

Structural basis of branch site recognition by the human spliceosome. Tholen J, Razew M et al. Science. 2022 Jan 7;375(6576):50-57.

Structure of pathological TDP-43 filaments from ALS with FTLD. Arseni D, Hasegawa M et al. Nature. 2022 Jan 6;601(7891):139–143.

Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants. McCallum M, Walls AC et al. Science. 2021 Dec 24;374(6575):1621-1626.

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News

December 8, 2021

The ChimeraX 1.3 production release is available. See the change log for what's new.

October 22, 2021

The ChimeraX 1.3 release candidate is available. Please try it and report any issues. See the change log for what's new.

May 28, 2021

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

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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

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

CaM-CaMKI peptide

Calmodulin and Target Peptide

Calmodulin (CaM) acts as a calcium sensor. When its four Ca++ sites are fully occupied, it binds and modulates the activity of various downstream proteins, including CaM-dependent protein kinase I (CaMKI). Here, a complex between CaM and its target peptide from CaMKI (PDB 1mxe) is shown with cartoons, a transparent molecular surface, silhouette outlines, and light soft ambient occlusion. (If you prefer a less smudgy/rustic appearance, try using light gentle instead.) For image setup other than positioning, see the command file cam.cxc.

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