2 results match your criteria: "University of Louisiana State University[Affiliation]"
Effects of the association of the α β lower legs on integrin ligand binding.
J Cell Biochem
August 2021
Department of Life Science, University of Louisiana State University, Baton Rouge, Louisiana, USA.
Article Synopsis
- Many integrins change shape to send signals, but it was not clear if integrin αβ does the same during activation.
- Researchers found that mutant forms of integrin αβ, which prevented the lower legs from separating, still bound to ligands as effectively as the normal version, indicating that ligand binding does not need this separation.
- They suggested that integrin αβ might only exist in an extended form with a closed headpiece, instead of changing configurations, and that this form could serve as a stable attachment point for ligands rather than transmitting signals across the cell membrane.
Atypical structure and function of integrin α β.
J Cell Physiol
July 2021
Department of Life Science, University of Louisiana State University, Baton Rouge, Louisiana, USA.
Article Synopsis
- Integrins are specialized proteins that help cells stick to one another and communicate signals across their membranes, with most having a shape that changes when active.
- Unlike other integrins, integrin β has a unique structure that lacks a key sequence for sending signals from inside the cell, indicating it may operate differently.
- Despite not changing shape when binding with ligands or metals, integrin β maintains a strong connection with targets, which makes it an unusual but effective member of the integrin family.