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1738: IL-7R Binder Redesign: Round 17

Closed since over 6 years ago

Intermediate

Summary


Created
September 29, 2019
Expires
Max points
100
Description

Note: This puzzle was closed early due to an error with the frozen binding helices. The puzzle has been reposted as Puzzle 1738b. Players will not be able to load solutions into the reposted puzzle.



Interleukin 7 receptor (IL-7R) is a protein that helps regulate the human immune system, and is an important target in cancer therapy research. In this puzzle, players start with two frozen helices bound to the IL-7R target (also frozen). Players can fold and design about 20 residues between the binding helices, with the goal of creating a well-folded protein that can bind the IL-7R target! Players may also redesign residues on the backside of the binding helices, but residues at the IL-7R interface are frozen in place. The most promising designs will have lots of helical and/or sheet structure with only short loops, and will have a well-packed, buried core. There are several Objectives in place; see the puzzle comments for details.



This is the 17th puzzle in the IL-7R binder series, meant to generate a large diversity of designs that can be tested in a high-throughput binding experiment! Due to time constraints, puzzles in this series will be online for only 4 days at a time. See the blog for more information. Remember, you can use the Upload for Scientists button for up to 5 designs that you want us to look at, even if they are not the best-scoring solutions!

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Comments


bkoep Staff Lv 1

Residue IE Score (max +500)
Monitors that all PHE, TYR, and TRP residues are scoring well.

Core Existence (max +1000)
Ensures that at least 25% of residues are buried in the protein core.

SS Design (max +400)
Penalizes all CYS residues. Penalizes GLY, ALA, SER, THR in helices. Penalizes GLY, ALA in sheets.

Residue Count (max +100)
Penalizes extra residues inserted beyond 110, at a cost of 20 points per residue. Players may use up to 115 residues in total.

NinjaGreg Lv 1

I like the connection at the two ends of the protein, but the two helices that should have been fixed can move,