Suggestions for new articles

From Proteopedia

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This page suggests molecules or topics for future articles in Proteopedia.

Nature, and perhaps other journals, allow comments from readers to be appended to scientific reports. Therefore, interactive 3D illustrations in Proteopedia, based on a report in Nature, can be linked to the online article in a comment.

Suggestions by Eric Martz

These suggestions are by User:Eric Martz, who invites anyone to start articles on these molecules. In cases where morphs can be done, Eric will be happy to provide technical help.

• 2012, January:
  • Krishnamurthy H, Gouaux E. X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature. 2012 Jan 9. doi: 10.1038/nature10737. PMID:22230955 doi:10.1038/nature10737
  • LeuT is a bacterial homolog of neurotransmitter sodium symporters that remove neurotransmitters from the synapse and terminate neurotransmission. New structures presented in this paper "establish a structural framework for the mechanism of neurotransmitter sodium symporters and their modulation by therapeutic and illicit substances".
  • A new substrate-free structure is outward-open, 3tt1. Comparison with a previous substrate-bound, outward occluded structure shows "how the binding of substrate closes the extracellular gate through local conformational changes".
  • A new substrate-free inward-open structure, 3tt3, involves large scale conformational changes.
  • The authors provide a supplementary true movie containing two morphs between three structures: substrate-free outward-open 3tt1 to leucine-bound, outward-occluded 2a65, and then to the inward-open 3tt3. Interactive morphs in Jmol could be advantageous.

• 2011, October:
  • Du J, Say RF, Lu W, Fuchs G, Einsle O. Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase. Nature. 2011 Oct 9. doi: 10.1038/nature10458. PMID:21983965 doi:10.1038/nature10458
• Fushinobu S, Nishimasu H, Hattori D, Song HJ, Wakagi T. Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase. Nature. 2011 Oct 9;478(7370):538-41. doi: 10.1038/nature10457. PMID:21983966 doi:10.1038/nature10457

• 2011, September:
  • Hansen SB, Tao X, Mackinnon R. Structural basis of PIP(2) activation of the classical inward rectifier K(+) channel Kir2.2. Nature. 2011 Aug 28. doi: 10.1038/nature10370. PMID:21874019 doi:10.1038/nature10370
  • "On PIP2 binding, a flexible expansion linker contracts to a compact helical structure, the cytoplasmic domain translates 6 Å and becomes tethered to the trans-membrane domain and the innner helix gate begins to open."
  • Probably suitable for a morph. The apo structure is 3jyc, and the PIP2-bound structure, 3spi. Supplementary information does not include any movies.