Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein

HIV-1 envelope glycoprotein (Env) mediates the fusion of viral and target cell membranes and is a major target for HIV vaccine development. Here, the authors determine the NMR structure of a bicelle incorporated Env segment comprising the transmembrane domain (TMD) and a portion of the cytoplasmic t...

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Autores principales: Alessandro Piai, Qingshan Fu, Yongfei Cai, Fadi Ghantous, Tianshu Xiao, Md Munan Shaik, Hanqin Peng, Sophia Rits-Volloch, Wen Chen, Michael S. Seaman, Bing Chen, James J. Chou
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/e13057d2254f431aa52b8fc7024ffbdf
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Sumario:HIV-1 envelope glycoprotein (Env) mediates the fusion of viral and target cell membranes and is a major target for HIV vaccine development. Here, the authors determine the NMR structure of a bicelle incorporated Env segment comprising the transmembrane domain (TMD) and a portion of the cytoplasmic tail (CT), and show that the CT folds into membrane attached amphipathic helices that wrap around the TMD thereby forming a support baseplate for the rest of Env, and they also provide insights into the dynamic coupling across the TMD between the ectodomain and CT.