Title :
Homo-oligomerization of transmembrane α-domain of integrin
Author :
Shamloo, Amir ; Nikbin, Ehsan ; Mehboudi, Nastaran ; Damirchi, Behzad
Author_Institution :
Dept. of Mech. Eng., Sharif Univ. of Technol., Tehran, Iran
Abstract :
Integrins contribute to form focal adhesions complex. Therefore, simulation of integrin interactions can be helpful in clarifying the mechanism of focal adhesion formation. Interactions of integrins can also initiate signal transduction in the focal adhesions. Since integrins contain α and β subunits that are separated in an active state, studying both subunits separately is crucial, since, in the active state of integrins, the distance between these subunits is long enough that they do not influence one another significantly. Thus, this study aims to investigate the tendency of α subunits of integrins to form homodimers. All simulations were carried out via MARTINI coarse grain (CG) molecular dynamics technique. α subunits were placed in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) lipid bilayer at a distance of 5 nm, and they were allowed to diffuse in the lipid bilayer. All simulations showed that α subunits have a tendency to form stable dimers.
Keywords :
biodiffusion; biological techniques; biomembrane transport; lipid bilayers; molecular biophysics; molecular dynamics method; proteins; α subunits; β subunits; 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine lipid bilayer; CG; MARTINI coarse grain molecular dynamics technique; POPC; distance 5 nm; focal adhesion complex; focal adhesion formation; homo-oligomerization; homodimer; integrin active state; integrin interactions; lipid bilayer diffusion; signal transduction; stable dimers; transmembrane α-domain; Adhesives; Biological system modeling; Biomembranes; Educational institutions; Lipidomics; Mechanical engineering; Proteins;
Conference_Titel :
Engineering in Medicine and Biology Society (EMBC), 2014 36th Annual International Conference of the IEEE
Conference_Location :
Chicago, IL
DOI :
10.1109/EMBC.2014.6943802