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, and the cell cycle. Here, the transmembrane and cytoplasmic (TMC) domains of integrin 1 and 1 were over-expressed and purified in detergent micelles. The structure and backbone relaxations of 1-TMC in LDAO micelles were determined and analyzed using solution NMR. A long helix, extending from the transmembrane region to the cytoplasmic tail, was observed in 1-TMC. 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 through several 1-TMC residues located at its N-terminal juxta-transmembrane region and C-terminal extended helix region.

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