ResearchPad - 511 https://www.researchpad.co Default RSS Feed en-us © 2020 Newgen KnowledgeWorks <![CDATA[Structural and functional insights into transmembrane AMPA receptor regulatory protein complexes]]> https://www.researchpad.co/article/elastic_article_15288 Fast excitatory neurotransmission is mediated by the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) subtype of ionotropic glutamate receptor (AMPAR). AMPARs initiate depolarization of the postsynaptic neuron by allowing cations to enter through their ion channel pores in response to binding of the neurotransmitter glutamate. AMPAR function is dramatically affected by auxiliary subunits, which are regulatory proteins that form various complexes with AMPARs throughout the brain. The most well-studied auxiliary subunits are the transmembrane AMPAR regulatory proteins (TARPs), which alter the assembly, trafficking, localization, kinetics, and pharmacology of AMPARs. Recent structural and functional studies of TARPs and the TARP-fold germ cell-specific gene 1-like (GSG1L) subunit have provided important glimpses into how auxiliary subunits regulate the function of synaptic complexes. In this review, we put these recent structures in the context of new functional findings in order to gain insight into the determinants of AMPAR regulation by TARPs. We thus reveal why TARPs display a broad range of effects despite their conserved modular architecture.

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<![CDATA[Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels]]> https://www.researchpad.co/article/Nde1cd7a3-65c6-48d3-b4f8-9f0851568715

High-resolution structural information is invaluable for understanding muscle function. Savich et al. use bifunctional spin labeling to determine the orientation of the myosin lever arm in muscle fibers at high resolution under ambient conditions, augmenting previous insights obtained from fluorescence and EM.

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<![CDATA[The voltage-gated sodium channel pore exhibits conformational flexibility during slow inactivation]]> https://www.researchpad.co/article/5c910777d5eed0c4841a4305

Voltage-gated sodium channels undergo slow inactivation during prolonged depolarization by means of a mechanism that is poorly understood. Chatterjee et al. study this process spectroscopically and reveal conformational flexibility of the pore region in the slow-inactivated state.

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<![CDATA[Structure, function, and allosteric modulation of NMDA receptors]]> https://www.researchpad.co/article/5c69ec8ed5eed0c48414de7a

Hansen et al. review recent structural data that have provided insight into the function and allosteric modulation of NMDA receptors.

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<![CDATA[Molecular determination of claudin-15 organization and channel selectivity]]> https://www.researchpad.co/article/5c368377d5eed0c4841f3e48

Members of the claudin family form tight junctions between adjacent epithelial and endothelial cells. Samanta et al. build an atomic model of claudin-15 using molecular dynamics simulations and conclude that four claudin-15 molecules each contribute an aspartic acid residue to form a selectivity filter.

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<![CDATA[Known structures and unknown mechanisms of TMEM16 scramblases and channels]]> https://www.researchpad.co/article/5c36836cd5eed0c4841f3c8c

Falzone et al. interpret the mechanisms underlying the activity of TMEM16 family members from recent structural and functional work.

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<![CDATA[Analysis of the quality of crystallographic data and the limitations of structural models]]> https://www.researchpad.co/article/5c01f8b8d5eed0c4842be84a

Arkhipova et al. caution that the limitations of structural models be taken into account when interpreting crystallographic data.

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<![CDATA[The structural basis of ryanodine receptor ion channel function]]> https://www.researchpad.co/article/5c01f8bad5eed0c4842be8b2

Meissner reviews progress toward our understanding of ryanodine receptor structure and function.

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<![CDATA[A new model for an old friend]]> https://www.researchpad.co/article/5c01f8c0d5eed0c4842be9db

JGP study suggests the anion exchanger AE1 operates via an elevator-like mechanism.

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