Main Page

Huddy, Hsia, Kibler, Xu & 27 others in the Nobel Prize winning group of David Baker have designed standardized protein building blocks that self assemble into a wide range of nanostructures. The building blocks attach to each other at engineered sites and angles, and come in various sizes.

>>> Get a quick overview! >>>

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 >>>

H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey. Scientific Reports 2016 doi: 10.1038/srep27399
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

>>> Visit this I3DC complement >>>

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 >>>