Structural highlights
Publication Abstract from PubMed
The design of protein sequences that fold into prescribed de novo structures is challenging. General solutions to this problem require geometric descriptions of protein folds and methods to fit sequences to these. The alpha-helical coiled coils present a promising class of protein for this and offer considerable scope for exploring hitherto unseen structures. For alpha-helical barrels, which have more than four helices and accessible central channels, many of the possible structures remain unobserved. Here, we combine geometrical considerations, knowledge-based scoring, and atomistic modeling to facilitate the design of new channel-containing alpha-helical barrels. X-ray crystal structures of the resulting designs match predicted in silico models. Furthermore, the observed channels are chemically defined and have diameters related to oligomer state, which present routes to design protein function.
Computational design of water-soluble alpha-helical barrels.,Thomson AR, Wood CW, Burton AJ, Bartlett GJ, Sessions RB, Brady RL, Woolfson DN Science. 2014 Oct 24;346(6208):485-8. doi: 10.1126/science.1257452. PMID:25342807[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Thomson AR, Wood CW, Burton AJ, Bartlett GJ, Sessions RB, Brady RL, Woolfson DN. Computational design of water-soluble alpha-helical barrels. Science. 2014 Oct 24;346(6208):485-8. doi: 10.1126/science.1257452. PMID:25342807 doi:http://dx.doi.org/10.1126/science.1257452