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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
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Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
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Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

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Mutational Insight into Allosteric Regulation of Kir Channel Activity.

Maryam Yekefallah1, Carver A Rasberry1, Evan J van Aalst1

  • 1Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas79409, United States.

ACS Omega
|December 12, 2022
PubMed
Summary

Researchers investigated the gating mechanism of Potassium (K+) channels using mutagenesis and simulations. They identified key residues involved in allosteric regulation and lipid interactions, offering insights into channel function and human Kir channel physiology.

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Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
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Area of Science:

  • Biophysics
  • Structural Biology
  • Molecular Physiology

Background:

  • Potassium (K+) channels are crucial for membrane potential, regulated by allosteric networks connecting inner and outer gates.
  • Inward-rectifier K+ (Kir) channels, like KirBac1.1, are ligand-gated by phosphatidylglycerol (PG) and are homologous to human Kir channels.

Purpose of the Study:

  • To investigate residues critical for KirBac1.1 gating and its allosteric network using site-directed mutagenesis.
  • To correlate structural changes and phosphatidylglycerol (PG) interactions with KirBac1.1 channel activity.

Main Methods:

  • Site-directed mutagenesis of KirBac1.1.
  • Fluorescence-based K+ and Na+ flux assays.
  • Coarse-grain molecular dynamics simulations.
  • Solid-state NMR (SSNMR) measurements.

Main Results:

  • Identified non-selective mutants with impaired function.
  • Observed altered PG-KirBac1.1 interactions and transmembrane helix contacts in mutants.
  • Established a link between lipid affinity, tryptophan residues, and a cationic pocket involving arginine residues.

Conclusions:

  • Mutated sites play a role in the proposed allosteric network governing KirBac1.1 gating.
  • Experimental and simulation data elucidate key residues in K+ channel gating and lipid allostery.
  • Findings have implications for human Kir channel physiology due to conserved residues.