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Structure of the human TRPM4 ion channel in a lipid nanodisc
TLDR
Two structures of full-length human TRPM4 embedded in lipid nanodiscs at ~3-angstrom resolution, as determined by single-particle cryo–electron microscopy reveal a general architecture for this major subfamily of TRP channels and a well-defined calcium-binding site within the intracellular side of the S1-S4 domain.
Structure and mechanism of Zn2+-transporting P-type ATPases
TLDR
The findings suggest a mechanistic link between PIB-type Zn2+-ATPases and PIII-type H+-ATORases and at the same time show structural features of the extracellular release pathway that resemble PII-type ATPases such as the sarcoplasmic/endoplasmsic reticulum Ca2-atPase (SERCA) and Na+, K+- ATPase.
Unbiased Simulations Reveal the Inward-Facing Conformation of the Human Serotonin Transporter and Na+ Ion Release
TLDR
Extended molecular dynamics simulations of an experimentally supported homology model of the human serotonin transporter with and without the natural substrate yielding a total of more than 1.5 µs of simulation of the protein dimer reveal a transition of hSERT from an outward-facing occluded conformation to an inward-facing conformation in a one-substrate-bound state.
Structure and Function of Cu(I)- and Zn(II)-ATPases.
TLDR
The Cu(I)- and Zn(II)-ATPases are compared, scrutinizing the molecular differences that allow transport of these two distinct metal types, and possible future directions of research in the field are discussed.
Controlling Styrene Maleic Acid Lipid Particles through RAFT.
TLDR
It is hypothesize that low dispersity copolymers, with control of polymer architecture are an ideal framework for the rational design of polymers for customized isolation and characterization of integral membrane proteins in native lipid bilayer systems.
Ligand Induced Conformational Changes of the Human Serotonin Transporter Revealed by Molecular Dynamics Simulations
TLDR
The results reveal that diverse conformations of the human serotonin transporter are captured from the molecular dynamics simulations depending on the type of the ligand bound, and that atomic-level understanding of how an inhibitor can dictate the conformational response of a transporter by ligand binding may be of great importance for future drug design.
Water-mediated interactions influence the binding of thapsigargin to sarco/endoplasmic reticulum calcium adenosinetriphosphatase.
TLDR
The hypothesis that four water molecules are present in the binding cavity of thapsigargin in sarco/endoplasmic reticulum calcium ATPase (SERCA) and mediate an extensive hydrogen-bonding network is verified by measuring the affinity of newly synthesized model compounds, which are prevented from participating in such water-mediated interactions as hydrogen- bond donors.
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