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Plos One : Structural Plasticity and Conformational Transitions of Hiv Envelope Glycoprotein Gp120, Volume 7

By Wu, Yuntao

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Book Id: WPLBN0003960385
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos One : Structural Plasticity and Conformational Transitions of Hiv Envelope Glycoprotein Gp120, Volume 7  
Author: Wu, Yuntao
Volume: Volume 7
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Historic
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Publisher: Plos

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Wu, Y. (n.d.). Plos One : Structural Plasticity and Conformational Transitions of Hiv Envelope Glycoprotein Gp120, Volume 7. Retrieved from http://www.ebooklibrary.org/


Description
Description : HIV envelope glycoproteins undergo large-scale conformational changes as they interact with cellular receptors to cause the fusion of viral and cellular membranes that permits viral entry to infect targeted cells. Conformational dynamics in HIV gp120 are also important in masking conserved receptor epitopes from being detected for effective neutralization by the human immune system. Crystal structures of HIV gp120 and its complexes with receptors and antibody fragments provide high-resolution pictures of selected conformational states accessible to gp120. Here we describe systematic computational analyses of HIV gp120 plasticity in such complexes with CD4 binding fragments, CD4 mimetic proteins, and various antibody fragments. We used three computational approaches : an isotropic elastic network analysis of conformational plasticity, a full atomic normal mode analysis, and simulation of conformational transitions with our coarse-grained virtual atom molecular mechanics (VAMM) potential function. We observe collective sub-domain motions about hinge points that coordinate those motions, correlated local fluctuations at the interfacial cavity formed when gp120 binds to CD4, and concerted changes in structural elements that form at the CD4 interface during large-scale conformational transitions to the CD4-bound state from the deformed states of gp120 in certain antibody complexes.

 

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