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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 Proteopedia presents this information in a user-friendly way as a collaborative & free 3D-encyclopedia of proteins & other biomolecules.
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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 >>>	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 >>>	Transport of Drugs & Nutrients Above is a transmembrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (shown above) opens and binds peptide or drug, then closes, while its cytoplasmic face (opposite end from the above) opens to release its cargo into the intestinal cell, which passes it on into the blood circulation. >>> See more animations and explanation >>>
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