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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
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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.
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Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
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Published on: August 9, 2019

Structure-function relationships of the polypyrimidine tract binding protein.

S D Auweter1, F H-T Allain

  • 1Institute for Molecular Biology and Biophysics, ETH Zürich, 8093, Zürich, Switzerland.

Cellular and Molecular Life Sciences : CMLS
|November 3, 2007
PubMed
Summary

Polypyrimidine tract binding protein (PTB) is crucial for mRNA metabolism. Structural studies reveal unusual features of PTB

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Published on: August 21, 2018

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Polypyrimidine tract binding protein (PTB) is a key RNA-binding protein.
  • PTB regulates critical mRNA metabolic processes, including splicing and translation.
  • PTB comprises four RNA recognition motifs (RRMs).

Purpose of the Study:

  • To review structural insights into PTB.
  • To elucidate PTB's mechanisms in RNA metabolism through structural analysis.
  • To highlight recent structural findings on PTB.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Small-angle X-ray scattering (SAXS).
  • Structural modeling of protein-peptide complexes.

Main Results:

  • Detailed structures of PTB RRMs in free and bound states were determined.
  • Unusual structural features of PTB were identified.
  • Structural data provides new insights into PTB's function in RNA processing.

Conclusions:

  • Structural information enhances understanding of PTB's role in mRNA metabolism.
  • PTB's unique structural characteristics are key to its regulatory functions.
  • Further research into PTB structure-function relationships is warranted.