Recently, scientists solvedthe solution structure of the transmembrane region and the cytoplasmic tail of integrin 1 in detergent micelles using NMR, and studied its interaction with the transmembrane region and the cytoplasmic tail of integrin 1 using chemical shift perturbation.This research provides the structuralbasisforfurther study of integrin 1/ 1mediated bidirectional cellular signaling pathways. This work was done by scientists in Hefei National Laboratory for Physical Science at Microscale, School of Life Sciences,USTC and High Magnetic Field Laboratory, CAS.

Integrin proteins are very important adhesion receptors that mediate cell-cell and cell-extracellular matrix interactions. They play essential roles in cell signaling and the regulation of cellular shape, motility,andthe cell cycle.Here, the structure ofthe transmembrane and cytoplasmicdomains(TMC) of integrin 1was determined using solution NMR, revealed a long -helix, extending from the transmembrane region to the cytoplasmic tail.Structural comparisons of 1-TMC with reported IIb-TMC domains indicated different conformations in the transmembrane regions and cytoplasmic tails. An NMR titration experiment indicated weak interactions between 1-TMC and 1-TMC.

Manuscript of this research entitled“Integrin 1 Has a Long Helix, Extending from the Transmembrane Region to the Cytoplasmic Tail in Detergent Micelles” was published online by PLOS ONE at May 1st, 2013 (DOI:10.1371/journal.pone.0062954).

Link to this article:http://www.plosone.org/article/info:doi/10.1371/journal.pone.0062954.