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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

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At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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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.
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Tumor suppressor genes are normal genes that can slow down cell division, repair DNA mistakes, or program the cells for apoptosis in case of irreparable damage. Hence, they play an essential role in preventing the proliferation of damaged cells.
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Single-Molecule FRET Imaging for Observing the Conformational Dynamics of Dynamin-Like GTPase Atlastin
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Conformational flexibility determines the Nf2/merlin tumor suppressor functions.

Marina C Primi1, Erumbi S Rangarajan1, Dipak N Patil1

  • 1Cell Adhesion Laboratory, Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter 33458, FL, United States.

Matrix Biology Plus
|August 2, 2021
PubMed
Summary

The Neurofibromatosis type 2 (NF2) protein, merlin, regulates cell proliferation by modulating the Hippo pathway. LATS1 binding to merlin causes an allosteric shift, impacting its tumor suppressor function in cancers.

Keywords:
ActinCancerCell adhesionCell junctionCell migrationCell signalingInositol phospholipidNeurofibromatosis type 2Plasma membrane

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Neurofibromatosis type 2 (NF2) gene encodes the Nf2/merlin tumor suppressor protein, crucial for regulating cell proliferation.
  • Nf2/merlin influences cell growth by modulating adhesive signaling pathways and oncogenic gene expression via the Hippo pathway.
  • The Hippo pathway, involving LATS kinase, YAP, and TAZ, controls contact inhibition and organ size.

Purpose of the Study:

  • To elucidate the structural mechanism of Nf2/merlin interaction with LATS1.
  • To provide mechanistic insights into how Nf2/merlin regulates the Hippo pathway.
  • To understand the implications for diseases, particularly cancer.

Main Methods:

  • High-resolution crystal structure determination of Nf2/merlin bound to LATS1.
  • Biochemical analysis of Nf2/merlin-LATS1 binding affinities.

Main Results:

  • The crystal structure reveals that LATS1 binding displaces the Nf2/merlin tail domain.
  • LATS1 binding induces an allosteric shift in the Nf2/merlin α-helix extending from the FERM domain.
  • Full-length Nf2/merlin binds LATS1 approximately 10-fold weaker than the Nf2/merlin-PIP2 complex.

Conclusions:

  • The study provides mechanistic insights into Nf2/merlin's role in the Hippo pathway.
  • Understanding Nf2/merlin-LATS1 interaction is critical for comprehending its tumor suppressor functions.
  • These findings are relevant to oncogenic features associated with various cancers.