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Publication Type : Journal Article
Thematic Areas : Center for Computational Engineering and Networking (CEN)
Source : Journal of Proteome Research, 16, 2017, 2936-2946
Url : https://pubmed.ncbi.nlm.nih.gov/34639046/
Campus : Coimbatore
School : Computational Engineering and Networking, School of Engineering
Center : Center for Computational Engineering and Networking, Computational Engineering and Networking
Verified : No
Year : 2021
Abstract : Here, we review recent molecular modelling and simulation studies of the Sec translocon, the primary component/channel of protein translocation into the endoplasmic reticulum (ER) and bacterial periplasm, respectively. Our focus is placed on the eukaryotic Sec61, but we also mention modelling studies on prokaryotic SecY since both systems operate in related ways. Cryo-EM structures are now available for different conformational states of the Sec61 complex, ranging from the idle or closed state over an inhibited state with the inhibitor mycolactone bound near the lateral gate, up to a translocating state with bound substrate peptide in the translocation pore. For all these states, computational studies have addressed the conformational dynamics of the translocon with respect to the pore ring, the plug region, and the lateral gate. Also, molecular simulations are addressing mechanistic issues of insertion into the ER membrane vs. translocation into the ER, how signal-peptides are recognised at all in the translocation pore, and how accessory proteins affect the Sec61 conformation in the co- and post-translational pathways.
Cite this Research Publication : Sreetama Das, Pratiti Bhadra, S. Ramakumar and Debnath Pal "Molecular Modeling of Signal Peptide Recognition by Eukaryotic Sec Complexes", Journal of Proteome Research, 16, 2017, 2936-2946