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PMID:25132083
Citation |
Lakomek, NA, Kaufman, JD, Stahl, SJ and Wingfield, PT (2014) HIV-1 envelope protein gp41: an NMR study of dodecyl phosphocholine embedded gp41 reveals a dynamic prefusion intermediate conformation. Structure 22:1311-1321 |
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Abstract |
Human immunodeficiency viral (HIV-1) fusion is mediated by the viral envelope gp120/gp41 complex (ENVelope glycoprotein). After gp120 shedding, gp41 is exposed and elicits membrane fusion via a cascade of conformational changes. In contrast to prefusion and postfusion conformation, little is known about any intermediate conformation. We report on a solution NMR investigation of homotrimeric HIV-1 gp41(27-194), comprising the transmembrane region and reconstituted in dodecyl phosphocholine (DPC) micelles. The protein is mainly α-helical, but experiences internal dynamics on the nanosecond and micro to millisecond time scale and transient α-helical behavior for certain residues in the N-terminal heptad repeat (NHR). Strong lipid interactions are observed, in particular for C-terminal residues of the NHR and imunodominant loop region connecting NHR and C-terminal heptad repeat (CHR). Our data indicate an extended conformation with features anticipated for a prefusion intermediate, presumably in exchange with a lowly populated postfusion six-helical bundle conformation. |
Links |
PubMed PMC4156547 Online version:10.1016/j.str.2014.06.016 |
Keywords |
Detergents/chemistry; HIV Envelope Protein gp41/chemistry; HIV-1/chemistry; Micelles; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Phosphorylcholine/analogs & derivatives; Phosphorylcholine/chemistry; Protein Structure, Quaternary; Protein Structure, Secondary; Virus Internalization |
Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|
enables |
GO:0042802: identical protein binding |
ECO:0000353: physical interaction evidence used in manual assertion |
UniProtKB:P04578:PRO_0000038428 |
F |
Seeded From UniProt |
complete | ||
Notes
See also
References
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