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Conformity01:20

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Conformity is the change in a person’s behavior to go along with the group, even if that person does not agree with the group.
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Conformations of Butane02:20

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Unlike ethane and propane that have only two major conformations, butane has more than two conformers. The staggered form of butane in which the bulky methyl groups on the two carbons are placed on opposite sides, that is, at a dihedral angle of 180°, is the lowest energy, most stable form — called the anti conformer. This conformation is stabilized due to the absence of steric repulsion between the largely spaced out methyl groups. The other two staggered conformations are...
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Conformations of Cycloalkanes02:29

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Adolf von Baeyer attempted to explain the instabilities of small and large cycloalkane rings using the concept of angle strain — the strain caused by the deviation of bond angles from the ideal 109.5° tetrahedral value for sp3  hybridized carbons. However, while cyclopropane and cyclobutane are strained, as expected from their highly compressed bond angles, cyclopentane is more strained than predicted, and cyclohexane is virtually strain-free. Hence, Baeyer’s theory that...
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Conformations of Cyclohexane02:11

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Updated: Feb 14, 2026

Wholemount Immunohistochemistry for Revealing Complex Brain Topography
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Fyn-Saracatinib Complex Structure Reveals an Active State-like Conformation.

Hai Minh Ta1, Banumathi Sankaran2, Eric D Roush3

  • 1Verna and Marrs McLean Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA.

International Journal of Molecular Sciences
|February 13, 2026
PubMed
Summary
This summary is machine-generated.

Saracatinib binds the Fyn kinase domain with low-nanomolar affinity. Structural analysis reveals an active-like conformation, offering insights for developing Fyn-selective inhibitors for neurodegenerative diseases.

Keywords:
AZD0530FynSrc-family kinaseTauTauopathyX-ray crystallographydasatinibkinase inhibitor selectivityneurodegenerationsaracatinibsurface plasmon resonance

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Structural Biology

Background:

  • Fyn kinase is crucial in neuroinflammation and synaptic dysfunction in Alzheimer's and Parkinson's diseases.
  • Saracatinib, a Src-family inhibitor, shows potential but lacks kinase selectivity due to conserved ATP-binding sites.

Purpose of the Study:

  • To structurally define saracatinib's interaction with the Fyn kinase domain.
  • To provide a basis for designing Fyn-selective inhibitors.

Main Methods:

  • Surface plasmon resonance (SPR) for binding kinetics.
  • X-ray crystallography to determine the Fyn kinase domain-saracatinib complex structure.

Main Results:

  • Saracatinib exhibits low-nanomolar affinity for Fyn kinase.
  • The crystal structure reveals an active-like Fyn conformation with saracatinib bound.
  • Saracatinib interacts with hinge and hydrophobic regions, with kinase-dependent αC-helix conformations.

Conclusions:

  • The active-like Fyn conformation presents a unique pocket for inhibitor design.
  • Structural insights facilitate the development of Fyn-selective inhibitors for neurodegenerative disorders.