Ion channel structure: Potassium channel structures

The molecular basis of K+ channel function is universally conserved. K+ channels allow K+ flux and are essential for the generation of electric current across excitable membranes. K+ channels are also the targets of various intracellular control mechanisms, such that the suboptimal regulation of channel function might be related to pathological conditions. Because of the fundamental role of K+ channels in controlling membrane excitability, a structural understanding of their function and regulation will provide a useful framework for understanding neuronal physiology. Many recent physiological and crystallographic studies have led to new insights into the workings of K+ channels.

[1]  M. Nanao,et al.  Voltage dependent activation of potassium channels is coupled to T1 domain structure , 2000, Nature Structural Biology.

[2]  Zhe Lu,et al.  Ion conduction pore is conserved among potassium channels , 2001, Nature.

[3]  B. Chait,et al.  The structure of the potassium channel: molecular basis of K+ conduction and selectivity. , 1998, Science.

[4]  W. N. Zagotta,et al.  Cyclic nucleotide-gated channels: shedding light on the opening of a channel pore , 2001, Nature Reviews Neuroscience.

[5]  C. Stevens,et al.  Crystal structure of the tetramerization domain of the Shaker potassium channel , 1998, Nature.

[6]  Y. Jan,et al.  An artificial tetramerization domain restores efficient assembly of functional Shaker channels lacking T1. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[7]  Roderick MacKinnon,et al.  Energetic optimization of ion conduction rate by the K+ selectivity filter , 2001, Nature.

[8]  D. Storm,et al.  Making New Connections Role of ERK/MAP Kinase Signaling in Neuronal Plasticity , 1999, Neuron.

[9]  J. Adelman,et al.  Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin , 2001, Nature.

[10]  H. Guy,et al.  NMR structure of inactivation gates from mammalian voltage-dependent potassium channels , 1997, Nature.

[11]  S. Ferroni,et al.  Structural Compatibility between the Putative Voltage Sensor of Voltage-gated K+ Channels and the Prokaryotic KcsA Channel* , 2001, The Journal of Biological Chemistry.

[12]  Britt Mellström,et al.  DREAM is a Ca2+-regulated transcriptional repressor , 1999, Nature.

[13]  Y. Jan,et al.  Putative receptor for the cytoplasmic inactivation gate in the Shaker K+ channel , 1991, Nature.

[14]  B. Roux,et al.  Energetics of ion conduction through the K + channel , 2022 .

[15]  Francisco Bezanilla,et al.  Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy , 1999, Nature.

[16]  Yoshihiro Kubo,et al.  Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel , 1993, Nature.

[17]  Detlef Bockenhauer,et al.  Potassium leak channels and the KCNK family of two-p-domain subunits , 2001, Nature Reviews Neuroscience.

[18]  B. Hille.  Ionic channels of excitable membranes , 2001 .

[19]  R. MacKinnon,et al.  Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors , 2001, Nature.

[20]  P. Biggin,et al.  Potassium channel structure: domain by domain. , 2000, Current opinion in structural biology.

[21]  Robert D. Finn,et al.  The Pfam protein families database , 2004, Nucleic Acids Res..

[22]  J. Sweatt,et al.  The A‐Type Potassium Channel Kv4.2 Is a Substrate for the Mitogen‐Activated Protein Kinase ERK , 2000, Journal of neurochemistry.

[23]  R. MacKinnon,et al.  Structure of a Voltage-Dependent K+ Channel β Subunit , 1999, Cell.

[24]  J. Buxbaum,et al.  Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment , 1998, Nature Medicine.

[25]  A. Hodgkin,et al.  A quantitative description of membrane current and its application to conduction and excitation in nerve , 1990 .

[26]  D. Wilkin,et al.  Neuron , 2001, Brain Research.

[27]  R. MacKinnon,et al.  Chemistry of ion coordination and hydration revealed by a K+ channel–Fab complex at 2.0 Å resolution , 2001, Nature.

[28]  Y. Jan,et al.  Specification of subunit assembly by the hydrophilic amino-terminal domain of the Shaker potassium channel. , 1992, Science.

[29]  G. Yellen,et al.  Gated Access to the Pore of a Voltage-Dependent K+ Channel , 1997, Neuron.

[30]  Bertil Hille,et al.  Voltage-Gated Ion Channels and Electrical Excitability , 1998, Neuron.

[31]  E. Perozo,et al.  Structural rearrangements underlying K+-channel activation gating. , 1999, Science.

[32]  K. Rhodes,et al.  Modulation of A-type potassium channels by a family of calcium sensors , 2000, Nature.

[33]  Xinghai Chen,et al.  Deletion analysis of K+ channel assembly , 1993, Neuron.

[34]  S. Choe,et al.  Towards the three-dimensional structure of voltage-gated potassium channels. , 1999, Trends in biochemical sciences.

[35]  F. Bezanilla,et al.  Negative Conductance Caused by Entry of Sodium and Cesium Ions into the Potassium Channels of Squid Axons , 1972, The Journal of general physiology.

[36]  I. Levitan,et al.  Association of Src Tyrosine Kinase with a Human Potassium Channel Mediated by SH3 Domain , 1996, Science.

[37]  E. Isacoff,et al.  Spectroscopic mapping of voltage sensor movement in the Shaker potassium channel , 1999, Nature.

[38]  Youxing Jiang,et al.  Structure of the RCK Domain from the E. coli K+ Channel and Demonstration of Its Presence in the Human BK Channel , 2001, Neuron.

[39]  O. Pongs,et al.  NIP domain prevents N-type inactivation in voltage-gated potassium channels , 1998, Nature.

[40]  Y. Jan,et al.  The Polar T1 Interface Is Linked to Conformational Changes that Open the Voltage-Gated Potassium Channel , 2000, Cell.