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<span style="font-size:2.0em; border:none; margin:0; padding:0.3em; color:#000; font-weight: bold;">Welcome to Proteopedia</span><br>
<span style="font-size:2.0em; border:none; margin:0; padding:0.3em; color:#000; font-weight: bold;">Welcome to Proteopedia</span><br>

Revision as of 07:23, 18 October 2018

Welcome to Proteopedia
ISSN 2310-6301 The free, collaborative 3D-encyclopedia of proteins & other molecules

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Geobacter pili: surprising function.

Y Gu, V Srikanth, AI Salazar-Morales, R Jain, JP O'Brien, SM Yi, RK Soni, FA Samatey, SE Yalcin, NS Malvankar. Nature 2021 doi: 10.1038/s41586-021-03857-w
Geobacter pili were long thought to be electrically conductive protein nanowires composed of PilA-N. Nanowires are crucial to the energy metabolism of bacteria flourishing in oxygen-deprived environments. To everyone's surprise, in 2019, the long-studied nanowires were found to be linear polymers of multi-heme cytochromes, not pili. The first cryo-EM structure of pili (2021) reveals a filament made of dimers of PilA-N and PilA-C, shown. Electrical conductivity of pili is much lower than that of cytochrome nanowires. Evidence suggests that PilA-NC filaments are periplasmic pseudopili crucial for exporting cytochrome nanowires onto the cell surface, rather than the pili serving as nanowires themselves.

>>> Visit I3DC Interactive Visualizations >>>

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Opening a Gate to Human Health

by Alice Clark (PDBe)
In the 1970s, an exciting discovery of a family of medicines was made by the Japanese scientist Satoshi Ōmura. One of these molecules, ivermectin, is shown in this artwork bound in the ligand binding pocket of the Farnesoid X receptor, a protein which helps regulate cholesterol in humans. This structure showed that ivermectin induced transcriptional activity of FXR and could be used to regulate metabolism.

>>> Visit this page >>>

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Coronavirus Spike Protein Priming

by Eric Martz
Coronavirus SARS-CoV-2 (responsible for COVID-19) has a spike protein on its surface, which enables it to infect host cells. Initially, proteases in the lungs clip the homo-trimeric spike protein at a unique sequence. This primes it, causing it to extend its receptor binding surface (shown in the above animation), optimizing binding to the host cell's ACE2 receptor (not shown). Next, spike protein initiates fusion of the virus and host cell membranes (not shown), enabling the virus RNA to enter the cell and initiate production of new virions. Knowledge of spike protein's molecular structure and function is crucial to developing effective therapies and vaccines.
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About this image
You Are What You Eat!

Above is an integral membrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (top) opens and binds peptide or drug (small solid object in the center), then closes, while its cytoplasmic face (bottom) opens to release its cargo into the intestinal cell, which passes it on to the blood circulation.

>>> See more animations and explanation >>>

Proteopedia Page Contributors and Editors (what is this?)

Jaime Prilusky

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