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DNA origami: 4 ring

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3D rendering of DNA origami for Mark Bathe lab at MIT. DNAs are programmed and self-assembled into precise 3D architectures, such as this four-layer ring, to organize synthetic chromophores and to replicate key aspects of bacterial photosynthetic systems. Reference: 1. Pan, K. et al. Lattice-free prediction of three-dimensional structure of programmed DNA assemblies. Nature communications

EGFR kinase domain in complex with Iressa

Constitutive activation of mutated EGFR (Epidermal Growth Factor Receptor) has been associated with a number of cancers, including lung cancer, anal cancers and glioblastoma multiforme. This 3D model reveals how Iressa (Gefitinib), the first selective inhibitor of EGFR tyrosine kinase domain, binds to EGFR. Reference: 1. Yun, C. H. et al. Structures of lung cancer-derived

Ubiquitin surrounded by water molecules

Ubiquitin is a small (8.5 kDa) regulatory protein that has been found in almost all tissues of eukaryotic organisms. The addition of ubiquitin to a substrate is called ubiquitination, a post-translational modification that affects proteins in many ways: it can signal for their degradation via the proteasome, alter their cellular location, affect their activity, and

Tobacco mosaic virus

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The first virus ever to be discovered: tobacco mosaic virus (TMV), a positive-sense single stranded RNA virus that infects a wide range of plants, especially tobacco and other members of the family Solanaceae. The infection causes characteristic mosaic-like mottling and discoloration on the leaves. TMV virion has a rod-like appearance, ~300 nm in length and ~18 nm in

Abl kinase domain in complex with imatinib

Imatinib (Glivec), a potent inhibitor of the constitutively activated Abl tyrosine kinase domain in the Bcr-Abl oncoprotein, shows remarkable clinical activity in patients of chronic myelogenous leukemia (CML). Reference: 1. Cowan-Jacob, S. W. et al. Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia. Acta crystallographica. Section D, Biological crystallography 63,

PPAR-gamma-RXR complex on DNA

The peroxisome proliferator-activated receptors (PPARs) form heterodimers with the retinoid X receptor (RXR), bind to DNA, and further regulate expression of many genes involved in energy utilization. Reference: 1. Chandra, V. et al. Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. Nature 456, 350-356, doi:10.1038/nature07413 (2008).