Crystal structure solved by protein folding game players

Online gamers have achieved a feat beyond the realm of Second Life or Dungeons and Dragons: they have deciphered the structure of an enzyme of an AIDS-like virus that had thwarted scientists for a decade. The article was published on Sunday in the journal Nature Structural & Molecular Biology, where – exceptionally in scientific publishing – both gamers and researchers are honoured as co-authors. Their target was a monomeric protease enzyme, a cutting agent in the complex molecular tailoring of retroviruses, a family that includes HIV.

They figured out the protein structure of a monomeric protease enzyme, which is “a cutting agent in the complex molecular tailoring of retroviruses, a family that includes HIV”. The understanding of this structure is an important step towards discovering the causes of many diseases related to this enzyme and coming up with treatments for them.

This is where Foldit comes in. Developed in 2008 by the University of Washington, it is a fun-for-purpose video game in which gamers, divided into competing groups, compete to unfold chains of amino acids – the building blocks of proteins – using a set of online tools. To the astonishment of the scientists, the gamers produced an accurate model of the enzyme in just three weeks. It is believed to be the first time that gamers have resolved a long-standing scientific problem.

 

One of Foldit’s creators, Seth Cooper, explained why gamers had succeeded where computers had failed.

People have spatial reasoning skills, something computers are not yet good at. Games provide a framework for bringing together the strengths of computers and humans. The results in this week’s paper show that gaming, science and computation can be combined to make advances that were not possible before.

Khatib, F., DiMaio, F., Cooper, S., Kazmierczyk, M., Gilski, M., Krzywda, S., Zabranska, H., Pichova, I., Thompson, J., Popović, Z., Jaskolski, M., & Baker, D. (2011). Crystal structure of a monomeric retroviral protease solved by protein folding game players Nature Structural & Molecular Biology DOI: 10.1038/nsmb.2119 [Free PDF]

[via SMH and TNW]

M-PMV retroviral protease structure improvement by the Foldit Contenders Group. (a) Progress of structure refinement over the first 16 d of game play. The x axis shows progression in time, and the y axis shows the Phaser log-likelihood (LLG) of each model in a near-native orientation. (b) Starting from a quite inaccurate NMR model (red), Foldit player spvincent generated a model (yellow) considerably more similar to the later determined crystal structure (blue) in the beta-strand region. © 2011 Nature America, Inc.

  • Marijab

    There is no science without art.