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Updated: Feb 22, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
Dynamics of allosteric modulation of lymphocyte function associated antigen-1 closure-open switch: unveiling the
Maryam Abdullahi1, Fisayo A Olotu1, Mahmoud E Soliman2,3,4
1Molecular Modeling and Drug Design Research, Group School of Health Sciences, University of KwaZulu- Natal, Westville Campus, Durban, 4001, South Africa.
Objectives:
To provide insight into the dynamics of the shape-shifting mechanistic events associated with the opening (activation) of Lymphocyte Function Associated Antigen-1 upon allosteric modulation by an activator, ICAM Binding Enhancer-667 (IBE-667), using molecular dynamics simulation.
Results:
Various parameters were used to appropriately describe and understand the sequence of events that characterized its activation across the simulation period such as residual distances, TriCα angles; as well as the dihedral angle. Our findings revealed a significant residual fluctuation and stability difference between both systems. Also, there was a synergistic coordination of the active MIDAS site by the downward pull of the α7 helix upon ligand binding, which appeared to be directly proportional to each other.
Conclusion:
Allosteric binding of IBE-667, activated LFA-1 integrin as evidenced by residual motion at the MIDAS region which appears to be synergistically coordinated by the downward pull of the α7 helix.
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