Ion Channel Collection

Anaesthetic inhibiting an ion channel C015 / 6718
Anaesthetic inhibiting an ion channel. Computer model showing the structure of propofol anaesthetic drug molecules (spheres)

MscL ion channel protein structure. Molecular model showing the protein structure of a Mechanosensitive Channel of Large Conductance (MscL) from a Mycobacterium tuberculosis bacterium

Potassium ion channel protein structure. Molecular model of a KcsA potassium ion (K+) channel from Streptomyces lividans bacteria

Potassium ion channel beta subunit. Molecular model showing the structure a beta subunit of a voltage-dependent potassium (K+) channel

KCNQ ion channel protein structure. Molecular model showing the protein structure of an ion channel domain. Ion channels are membrane-spanning proteins that form a pathway for the movement of

Potassium ion channel cavity structure. Molecular model showing the structure of a cavity formed by potassium ion channel proteins

MscS ion channel protein structure F006 / 9650
MscS ion channel protein structure. Molecular model of a mechanosensitive channel of small conductance (MscS) from an Escherichia coli bacterium

Voltage-gated potassium channel F006 / 9642
Voltage-gated potassium channel. Molecular model of a voltage-gated potassium (Kv) ion channel. Ion channels are membrane-spanning proteins that form pores in cell membranes

MscS ion channel protein structure F006 / 9626
MscS ion channel protein structure. Molecular model of a mechanosensitive channel of small conductance (MscS) from an Escherichia coli bacterium

MscL ion channel protein structure F006 / 9624
MscL ion channel protein structure. Molecular model of a mechanosensitive channel of large conductance (MscL) from a Mycobacterium tuberculosis bacterium

Voltage-gated potassium channel F006 / 9562
Voltage-gated potassium (Kv) ion channel, molecular model. Ion channels are membrane-spanning proteins that form pores in cell membranes

Outer membrane receptor protein molecule F006 / 9398
Outer membrane receptor protein. Molecular model of FecA an outer membrane receptor protein

Voltage-gated potassium channel F006 / 9391
Voltage-gated potassium channel. Molecular model of a voltage-gated potassium (Kv) ion channel complexed with the antigen-binding fragment (Fab) of a monoclonal antibody

Voltage-gated potassium channel F006 / 9324
Voltage-gated potassium channel. Molecular model of a voltage-gated potassium (Kv) ion channel. Ion channels are membrane-spanning proteins that form pores in cell membranes

Ketamine drug binding to ion channel, molecular model. Several molecules of the drug ketamine binding to a pentameric ligand-gated ion channel (pLGIC)

MscS ion channel protein structure. Molecular model showing the protein structure of a Mechanosensitive Channel of Small Conductance (MscS) from an Escherichia coli bacterium

Influenza proton pump, molecular model
Influenza proton pump. Molecular model showing the protein structure of a proton pump from an influenza virus. Proton pumps are membrane proteins that move protons across a cell membrane

Chloride ion channel, molecular model. This is a ClC ion channel. Its role is to mediate the flow of chloride ions across cell membranes

Potassium ion channel. Computer artwork of a KcsA potassium ion (K+) channel (ribbons) embedded in a phospholipid (spheres) cell membrane (horizontal, centre)

Voltage-gated potassium channel. Computer model showing the molecular structure of a voltage-gated potassium (Kv) ion channel

Anaesthetic inhibiting an ion channel C015 / 6723
Anaesthetic inhibiting an ion channel. Computer model showing the structure of propofol anaesthetic drug molecules (spheres) bound to a pentameric ligand-gated ion channel (pLGIC, blue ribbons)

Anaesthetic inhibiting an ion channel C015 / 6722
Anaesthetic inhibiting an ion channel. Computer model showing the structure of propofol anaesthetic drug molecules (spheres) bound to a pentameric ligand-gated ion channel (pLGIC, blue ribbons)

Anaesthetic inhibiting an ion channel C015 / 6720
Anaesthetic inhibiting an ion channel. Computer model showing the structure of propofol anaesthetic drug molecules (lower left and right) bound to a pentameric ligand-gated ion channel (pLGIC, grey)

Anaesthetic inhibiting an ion channel C015 / 6721
Anaesthetic inhibiting an ion channel. Computer model showing the structure of propofol anaesthetic drug molecules (spheres)

Anaesthetic inhibiting an ion channel C015 / 6719
Anaesthetic inhibiting an ion channel. Computer model showing the structure of propofol anaesthetic drug molecules (spheres)

Ionotropic glutamate receptor C015 / 5813
Ionotropic glutamate receptor, molecular model. When glutamate binds to this receptor, it opens up trans-membrane ion channels vital for the functioning of the nervous system

Ionotropic glutamate receptor C015 / 5812
Ionotropic glutamate receptor, molecular model. When glutamate binds to this receptor, it opens up trans-membrane ion channels vital for the functioning of the nervous system

Sodium V-ATPase rotor ring C015 / 5379
Sodium V-ATPase rotor ring, molecular model. V-ATPases (vacuolar-type ATPase) are evolutionarily ancient enzymes that helps transport ions across cell membranes

Sodium V-ATPase rotor ring C015 / 5378
Sodium V-ATPase rotor ring, molecular model. V-ATPases (vacuolar-type ATPase) are evolutionarily ancient enzymes that helps transport ions across cell membranes

Plant anion channel protein homologue C016 / 2555
Plant anion channel protein homologue, molecular model. Obtained from the bacterium Haemophilus influenzae, this anion channel protein (TehA) is being studied due to its common structure (homologue)

Plant anion channel protein homologue C016 / 2556
Plant anion channel protein homologue, molecular model. Obtained from the bacterium Haemophilus influenzae, this anion channel protein (TehA) is being studied due to its common structure (homologue)

Potassium channel molecule. Molecular model of a KcsA potassium ion (K+) channel molecule from Streptomyces lividans bacteria

Potassium channel molecule C013 / 8878
Potassium channel molecule. Computer model showing the secondary structure of a KcsA potassium ion (K+) channel molecule from Streptomyces lividans bacteria

Cell membrane, artwork C013 / 4988
Cell membrane. Computer artwork of a section through an animal cell showing transmembrane proteins in the cell membrane. The membrane of the cell consists of a dual layer of phospholipids (dark blue)

Cell membrane, artwork C013 / 4986
Cell membrane. Computer artwork of a section through an animal cell showing transmembrane proteins in the cell membrane. The membrane of the cell consists of a dual layer of phospholipids (dark blue)

Potassium channel molecular model
Potassium channel research. Molecular model of the molecular structure of a KcsA potassium ion (K+) channel (brown spirals, centre) from a mouse (mus musculus)

Nerve impulse propagation, diagram
Nerve impulse propagation. Diagram showing the mechanism of propagation of the action potential (spike in voltage) which is known as a nerve impulse

Synapse structure, artwork
Synapse structure. Cutaway artwork showing the structure of a synapse, the point where two nerve ending meet. The electrical impulse moving along a nerve is transmitted to the adjacent nerve by

Animal cell processes, artwork
Animal cell processes. Cutaway artwork showing the structures inside an animal cell and four different processes that take place inside it or on its membrane (all marked by magnifying glasses)

Influenza virus structure, 3D artwork
Influenza virus structure. 3D computer artwork showing the structure of a generic influenza virion. A portion of the virions protein coat (capsid) has been cut away

Influenza virus structure, artwork
Influenza virus structure, cutaway artwork. The core of the virus is its genetic material, here 8 coloured ribbons of single-stranded RNA (ribonucleic acid)

Flu virion protein assembly, artwork. Three types of flu membrane (surface) proteins are shown coming together here to form the coating for a new virion

Blocked flu virus ion channel, artwork. This ion channel is an M2 membrane ion channel, found in the membranes of flu viruses

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"Ion Channels: Unlocking the Secrets of Cellular Communication" Ion channels play a crucial role in various physiological processes, and their intricate structures hold fascinating secrets. One such example is an anaesthetic inhibiting an ion channel (C015/6718), which sheds light on how these channels can be modulated for medical purposes. The MscL ion channel protein structure reveals its unique architecture, allowing it to respond to mechanical stress and regulate osmotic pressure within cells. On the other hand, the potassium ion channel protein structure showcases its selective permeability to potassium ions, vital for maintaining cellular homeostasis. Delving deeper into potassium ion channels, we discover the importance of the beta subunit in fine-tuning their activity. This subunit acts as a regulatory component that modifies channel kinetics and enhances their functionality. Another intriguing member of this family is the KCNQ ion channel protein structure. Its distinct arrangement enables it to control neuronal excitability and plays a critical role in hearing and epilepsy. Exploring further, we encounter the MscS ion channel protein structure (F006/9650). This mechanosensitive channel responds to membrane tension changes by opening or closing, ensuring cell survival under varying environmental conditions. Intriguingly, studying the cavity structure within potassium ion channels provides insights into how ions navigate through these narrow pathways while maintaining selectivity and efficient transport across cell membranes. Continuing our journey through structural wonders, we revisit MscL's protein structure (F006/9624) alongside MscS's counterpart (F006/9626). These two proteins demonstrate remarkable adaptability in responding to different stimuli while preserving cellular integrity. Lastly, let us not forget about voltage-gated potassium channels (F006/9642), responsible for generating action potentials in excitable cells like neurons and muscle fibers. Their precise conformation allows them to open or close upon changes in membrane potential with exceptional speed and accuracy.