1590c: Aflatoxin Challenge: Round 11
Closed since over 7 years ago
Intermediate Overall DesignSummary
- Created
- October 24, 2018
- Expires
- Max points
- 100
Note: This puzzle replaces Puzzle 1590b, which had some intermittent scoring problems. Players may load in solutions saved from Puzzle 1590b.
Redesign the active site to bind aflatoxin! This is Round 11 of the Aflatoxin Challenge. Since the last round, the Siegel Lab has introduced a few mutations in the active site, which might allow for some new redesign. This time, we're asking players to focus on just one loop of the starting structure, which clashes with the aflatoxin ligand in the binding pocket. Players may insert up to 20 extra residues into the designable loop, at a cost of 20 points per residue. Parts of the scaffold protein have been trimmed to reduce the size of the puzzle, and we've upweighted ligand interactions by a factor of five. We'd like to see if Foldit players can design proteins that make more interactions with the ligand! See the blog for more details.
Aflatoxins are a class of poisonous compounds that contaminate a significant portion of the global food supply. In this puzzle, players are challenged to redesign an enzyme that could break down aflatoxin molecules. The majority of the protein is frozen, with the aflatoxin ligand fixed in a binding pocket. Surrounding the binding pocket are a number of loops that might be redesigned without affecting the folding stability of the protein. In these loops, players may manipulate the protein backbone and mutate the residue sidechains. Redesign the loops of this protein to better bind the aflatoxin ligand!
This is the eleventh puzzle of our Aflatoxin Challenge, sponsored by Mars Inc. and Thermo Fisher Scientific. Promising designs will be tested by the Siegel Lab at UC Davis. By participating in the challenge/game, the players agree that all player designs will be available permanently in the public domain, and the players will not seek intellectual property protection over the designs created as part of the challenge/game.
