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Ion channels: structure and function
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Current research | Resources | Archive
Ion channels allow the movement of ions across cell membranes, and therefore fundamental physiological processes such as muscle contraction. In 1998, we saw for the first time what an ion channel actually looks like in a paper describing the crystal structure of a potassium channel. Now we have an array of ion channel structures, which we exemplify in this regularly updated collection of papers that illustrate the structural revolution that the field is currently experiencing.
Current research
ARTICLES
Structural mechanism of plant aquaporin gating
Susanna Törnroth-Horsefield et al.
Plants counteract fluctuations in water supply by regulating all aquaporins in the cell plasma membrane. Channel closure results either from the dephosphorylation of two.
Nature AOP, (07 December 2005) doi:10.1038/nature04316
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Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
Tamir Gonen et al.
Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. Here we describe a 1.9 � resolution structure.
Nature 438, 633–638 (01 December 2005) doi:10.1038/nature04321
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NEWS AND VIEWS
Cell biology: A greasy grip
Anthony G. Lee
How do the lipids and proteins of the cell membrane interact to create a functioning barrier for the cell? A high-resolution structure of a membrane
Nature 438, 569–570 (01 December 2005) doi:10.1038/438569a
Top of pageResources
- Nature Structural Biology
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- Nature Reviews Neuroscience
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Archive
NEWS FEATURE
Ion channel structures: They said it couldn't be done...
Alison Abbott
Nature 418, 268–269 (18 July 2002) doi:10.1038/418268a
REVIEW
The voltage-gated potassium channels and their relatives
Gary Yellen
Nature 419, 35–42 (05 September 2002) doi:10.1038/nature00978
LETTERS
Structure and different conformational states of native AMPA receptor complexes
Terunaga Nakagawa et al.
Ionotropic glutamate receptors mediate fast excitatory synaptic transmission in the central nervous system.
Nature 433, 545–549 (03 February 2005) doi:10.1038/nature03328
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Electron microscopic analysis of KvAP voltage-dependent K+ channels in an open conformation
Qiu-Xing Jiang et al.
Nature 430, 806–810 (12 August 2004) doi:10.1038/nature02735
Structure of a complex between a voltage-gated calcium channel β-subunit and an α-subunit domain
Filip Van Petegem et al.
Nature 429, 671–675 (10 June 2004) doi:10.1038/nature02588
Structural basis of the α1-β subunit interaction of voltage-gated Ca2+ channels
Yu-hang Chen et al.
Nature 429, 675–680 (10 June 2004) doi:10.1038/nature02641
Aquaporin-0 membrane junctions reveal the structure of a closed water pore
Tamir Gonen et al.
Nature 429, 193–197 (13 May 2004) doi:10.1038/nature02503
ARTICLES
Subunit arrangement and function in NMDA receptors
Hiroyasu Furukawa et al.
Excitatory neurotransmission mediated by NMDA (N-methyl-d-aspartate) receptors is fundamental to the physiology of the mammalian central nervous system. These receptors are heteromeric ion channels.
Nature 438, 185–192 (10 November 2005) doi:10.1038/nature04089
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Structure and gating mechanism of the acetylcholine receptor pore
Atsuo Miyazawa et al.
Nature 423, 949–955 (26 June 2004) doi:10.1038/nature01748
X-ray structure of a voltage-dependent K+ channel
Youxing Jiang et al.
Nature 423, 33–41 (01 May 2003) doi:10.1038/nature01580
The principle of gating charge movement in a voltage-dependent K+ channel
Youxing Jiang et al.
Nature 423, 42–48 (01 May 2003) doi:10.1038/nature01581
Open channel structure of MscL and the gating mechanism of mechanosensitive channels
Eduardo Perozo et al.
Nature 418, 942–948 (29 August 2002) doi:10.1038/nature00992
Crystal structure and mechanism of a calcium-gated potassium channel
Youxing Jiang et al.
Nature 417, 515–522 (30 May 2002) doi:10.1038/417515a
Mechanism of glutamate receptor desensitization
Yu Sun et al.
Nature 417, 245–253 (16 May 2002) doi:10.1038/417245a
X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion
Raimund Dutzler et al.
Nature 415, 287–294 (17 January 2002) doi:10.1038/415287a
Structural basis of water-specific transport through the AQP1 water channel
Haixin Sui et al.
Nature 414, 872–878 (20 December 2001) doi:10.1038/414872a
Energetic optimization of ion conduction rate by the K+ selectivity filter
João H. Morais-Cabral et al.
Nature 414, 37–42 (01 November 2001) doi:10.1038/414037a
Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution
Yufeng Zhou et al.
Nature 414, 43–48 (01 November 2001) doi:10.1038/414043a
Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors
Ming Zhou et al.
Nature 411, 657–661 (07 June 2001) doi:10.1038/411657a
Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
Katjuša Brejc et al.
Nature 411, 269–276 (17 May 2001) doi:10.1038/411269a
NEWS & VIEWS
Structure and gating mechanism of the acetylcholine receptor pore
Atsuo Miyazawa et al.
Nature 423, 949–955 (26 June 2004) doi:10.1038/nature01748
Structural biology: Life's transistors
Fred J. Sigworth
Nature 423, 21–22 (1 May 2003) doi:10.1038/423021a
Ion channels: An open and shut case
Maria Schumacher and John P. Adelman
Nature 417, 501–502 (30 May 2002) doi:10.1038/417501a
Cell biology: Chloride channels are different
Thomas J. Jentsch
Nature 415, 276–277 (17 January 2002) doi:10.1038/415276a
See potassium run
Christopher Miller
Nature 414, 23–24 (01 November 2001) doi:10.1038/414023a
Fifty years of inactivation
Richard W. Aldrich
Nature 411, 643–644 (07 June 2001) doi:10.1038/411643a
