Structural Plasticity and Conformational Transitions of HIV Envelope Glycoprotein gp120
نویسندگان
چکیده
منابع مشابه
Structural Plasticity and Conformational Transitions of HIV Envelope Glycoprotein gp120
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 str...
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The HIV-1 envelope glycoprotein is a trimeric complex of heterodimers composed of a surface glycoprotein, gp120, and a transmembrane component, gp41. The association of this complex with CD4 stabilizes the coreceptor-binding site of gp120 and promotes the exposure of the gp41 helical region 1 (HR1). Here, we show that a 15-amino-acid peptide mimetic of the HIV-1 coreceptor CCR5 fused to a dimer...
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The x-ray crystal structure of the gp120 core derived from the HXBc2 strain of HIV-1, in a ternary complex with two-domain CD4 and a neutralizing antibody, has been solved [1]. The gp120 core contains deletions of the V1, V2 and V3 variable loops and of the Nand C-termini, compared with full-length gp120. The implications of this structure for understanding the interaction of the HIV-1 envelope...
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ژورنال
عنوان ژورنال: PLoS ONE
سال: 2012
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0052170