Protein structures spelling "MOL BIO." The underlying gimmick behind this design is that each structure is relevant to research that was/is being done by faculty at Princeton. (Special thanks to Kalina Tsolova who helped greatly in brainstorming and choosing the structures!)
M - The glucose transporter GLUT3. The structure of this specific conformation was elucidated in a paper published by Nieng Yan.
O - Nocturnin, a metabolic protein expressed in tune with the circadian rhythm. The Korennykh lab recently identified that NADP+/NADPH are its substrates.
L - Vps33. A protein that interacts with SNARE complexes required for membrane fusion within cells. This structure was elucidated by the Hughson lab.
B - The PP2A phosphatase activator, a regulatory protein with many far reaching effects. Jeffry B. Stock's lab researches its role in neurodegenerative diseases.
I - qRRM1 (quasi-RNA recognition motif) of the Drosophila protein Glorund, which regulates RNA translation. The Gavis lab found that Glorund has multiple modes of binding RNA, using this ability to expand its repertoire of functions.
O - Tryptophan decarboxylase from the gut bacteria Ruminococcus gnavus. It was identified in a human microbiome study authored by Mohamed S. Donia, who is interested in how activities of enzymes such as these may affect human hosts.
The protein structures were traced over from 3D models available in the RSCB PDB (Protein Data Bank). PDB images and data are freely available for usage, provided there is proper attribution.
