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Related Concept Videos

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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Cooperative Binding of Transcription Regulators02:13

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Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
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COP Coated Vesicles00:59

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Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
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Related Experiment Video

Updated: Dec 17, 2025

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
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Functional (un)cooperativity in elevator transport proteins.

Katharina Holzhüter1, Eric R Geertsma2

  • 1Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue Str. 9, D-60438 Frankfurt am Main, Germany.

Biochemical Society Transactions
|June 24, 2020
PubMed
Summary
This summary is machine-generated.

Enzymes regulate their own activity through cooperativity, where protein sites interact to control reaction rates. This review focuses on cooperativity in elevator-type membrane transporters.

Keywords:
elevator alternating-access mechanisminterprotomer cooperativitymembrane deformationmembrane transportquarternary statesolute carrier

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Area of Science:

  • Biochemistry and Molecular Biology
  • Membrane Transport Mechanisms

Background:

  • Enzyme activity is regulated through various mechanisms.
  • Cooperativity, an intrinsic protein behavior, modulates enzyme reaction rates without external factors.
  • Both soluble and membrane proteins exhibit cooperativity.

Purpose of the Study:

  • To review interprotomer cooperativity in elevator-type membrane transporters.
  • To highlight key examples and experimental methodologies.

Main Methods:

  • Literature review of existing research on protein cooperativity.
  • Analysis of elevator-type transporter structures and functions.

Main Results:

  • Cooperativity is a significant intrinsic regulatory mechanism for enzymes.
  • Elevator-type transporters, characterized by large perpendicular movements, display interprotomer cooperativity.
  • Various experimental approaches are employed to study this phenomenon.

Conclusions:

  • Interprotomer cooperativity is crucial for the function of elevator-type membrane transporters.
  • Understanding cooperativity enhances knowledge of enzyme regulation and transport mechanisms.