Journal
SCIENCE
Volume 346, Issue 6208, Pages 485-488Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1257452
Keywords
-
Categories
Funding
- U.K. Biotechnology and Biological Sciences Research Council (BBSRC) South West Doctoral Training Partnership
- Engineering and Physical Sciences Research Council (EPSRC) Bristol Chemical Synthesis Centre for Doctoral Training
- EPSRC [EP/J001430/1]
- BBSRC [BB/J008990/1]
- European Research Council [340764]
- Royal Society Wolfson Research Merit Award
- Diamond Light Source [MX8922]
- Biotechnology and Biological Sciences Research Council [1228976, BB/J008990/1, BB/L01386X/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [1115150, EP/J001430/1, EP/K03927X/1] Funding Source: researchfish
- BBSRC [BB/L01386X/1, BB/J008990/1] Funding Source: UKRI
- EPSRC [EP/K03927X/1, EP/J001430/1] Funding Source: UKRI
Ask authors/readers for more resources
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 a-helical coiled coils present a promising class of protein for this and offer considerable scope for exploring hitherto unseen structures. For a-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 a-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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available