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Suggestions for new articles

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(Suggestions by Eric Martz)
(Suggestions by Eric Martz)
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*2012, January: <ref group="xtra">PMID: 22230955</ref><references group="xtra"/>
*2012, January: <ref group="xtra">PMID: 22230955</ref><references group="xtra"/>
-
**LeuT is a bacterial homolog of neurotransmitter sodium symporters that remove neurotransmitters from the synapse and terminate neurotransmission.
+
**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
+
**A new substrate-free structure is outward-open, [[3tt1]]. Comparison with a previous substrate-bound, outward occluded structure show "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 [[Morphs#True_Movies|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, September: <ref group="xtra">PMID: 21874019</ref><references group="xtra"/>
* 2011, September: <ref group="xtra">PMID: 21874019</ref><references group="xtra"/>
** "On PIP2 binding, a flexible expansion linker contracts to a compact helical structure, the cytoplasmic domain translates 6 &Aring; and becomes tethered to the trans-membrane domain and the innner helix gate begins to open."
** "On PIP2 binding, a flexible expansion linker contracts to a compact helical structure, the cytoplasmic domain translates 6 &Aring; 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.
** Probably suitable for a morph. The apo structure is [[3jyc]], and the PIP2-bound structure, [[3spi]]. Supplementary information does not include any movies.

Revision as of 16:02, 24 March 2012

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

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 show "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, 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.

Proteopedia Page Contributors and Editors (what is this?)

Eric Martz, Karsten Theis

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