2017
DOI: 10.1016/j.str.2017.09.010
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Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein

Abstract: SUMMARY The cytoplasmic tail of gp41 (gp41CT) remains the last HIV-1 domain with an unknown structure. It plays important roles in HIV-1 replication such as mediating envelope (Env) intracellular trafficking and incorporation into assembling virions, mechanisms of which are poorly understood. Herein, we present the solution structure of gp41CT in a micellar environment and characterize its interaction with the membrane. We show that the N-terminal 45 residues are unstructured and not associated with the membra… Show more

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citations
Cited by 47 publications
(62 citation statements)
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References 72 publications
(101 reference statements)
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“…The inter-helical distances at the MPER and CT sequences reflect the differing ability of these regions to open and allow the entry of water and ions into the trimer core (see below). The MPER region remains very stable and tightly packed with stable COM distances between neighboring peptides (~1.2 nm), consistent with experimental observations of the known α-helical character of MPER peptides (65), residue-specific NMR relaxation rates (24), and the observed flexibility of CT residues 707-751 (69). Minor increases in COM distance were observed in the MPER region, persisting for at most 100 ns before returning to a tightly packed state ( Figure S7).…”
Section: Dynamics Of the Tmdsupporting
confidence: 85%
“…The inter-helical distances at the MPER and CT sequences reflect the differing ability of these regions to open and allow the entry of water and ions into the trimer core (see below). The MPER region remains very stable and tightly packed with stable COM distances between neighboring peptides (~1.2 nm), consistent with experimental observations of the known α-helical character of MPER peptides (65), residue-specific NMR relaxation rates (24), and the observed flexibility of CT residues 707-751 (69). Minor increases in COM distance were observed in the MPER region, persisting for at most 100 ns before returning to a tightly packed state ( Figure S7).…”
Section: Dynamics Of the Tmdsupporting
confidence: 85%
“…In this study, we used NMR to obtain high-resolution information of the HIV-1 Env CT folding in the context of the TMD and lipid bilayer. We find that the CT adopts a structure different from the previous model 19 that can explain the physical coupling between the CT and the ectodomain.…”
contrasting
confidence: 72%
“…1a). The LLP2 is not a long continuous helix as previously proposed 19 ; instead it forms two helices, designated H1 (residues 741-764) and H2 (residues 769-786), adopting a ring-like structure around the C-terminal region of the TMD trimer. The three H1s make direct contacts with the TMD trimer to form an inner ring around the TMD (Fig.…”
Section: Resultsmentioning
confidence: 72%
See 1 more Smart Citation
“…We chose an approximate azimuthal orientation based on connections emanating from the C-terminal helices of the BG505 SOSIP.664 model ( Fig. 2B) The CT, which includes several membrane-associated, amphipathic helices [35], is completely disordered, as expected in the absence of a lipid bilayer.…”
Section: Model Buildingmentioning
confidence: 99%