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ISSN 2310-6301 As life is more than 2D, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules Often it is difficult to utilize the wealth of information found in 3D biomacromolecular structures. Proteopedia's goal is to present structure/function information on these molecules in a user-friendly manner to a broad scientific audience.
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HIV-1 protease by David Canner The X-ray structure of HIV-1 protease reveals that it is composed of two symmetrically related subunits which form a tunnel where they meet. This is critical because it contains the active site of the protease, consisting on two Asp-Thr-Gly conserved sequences, making it a member of the aspartyl protease family. The two catalytic Asp's either interact with the incoming water or protonate the carbonyl to make the carbon more electrophilic for the incoming water. >>> Visit this page >>>	Molecular Sculpture by Eric Martz A historical review on sculptures and physical models of macromolecules. >>> Visit this page >>>	Structure of Anticancer Ruthenium Half-Sandwich Complex Bound to Glycogen Synthase Kinase 3ß G Atilla-Gocumen, L Di Costanzo, E Meggers. J Biol Inorg Chem. 2010 doi: 10.1007/s00775-010-0699-x A crystal structure of an organometallic half-sandwich ruthenium complex bound to glycogen synthase kinase 3ß (GSK-3ß) reveals that the inhibitor binds to the ATP binding site via an induced fit mechanism utilizing several hydrogen bonds and hydrophobic interactions. Importantly, the metal is not involved in any direct interaction with the protein kinase but fulfills a purely structural role. >>> Visit this I3DC complement >>>	Touch-Sensitive Channel Touching stretches cell membranes, opening mechanosensitive ion channels, leading to sensation by the nervous system. Pictured is the transmembrane region of a similar channel in bacteria. When closed, the narrow opening is lined by hydrophobic amino acid sidechains, making it non-conductive to ions. >>> See more animations and explanation >>>
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Jaime Prilusky, Joel L. Sussman, Angel Herraez