The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Entropic switch regulates myristate exposure in the HIV-1 matrix protein
Open accessAbstract
The myristoylated matrix protein (myr-MA) of HIV functions as a regulator of intracellular localization, targeting the Gag precursor polyprotein to lipid rafts in the plasma membrane during virus assembly and dissociating from the membrane during infectivity for nuclear targeting of the preintegration complex. Membrane release is triggered by proteolytic cleavage of Gag, and it has, until now, been believed that proteolysis induces a conformational change in myr-MA that sequesters the myristyl group. NMR studies reported here reveal that myr-MA adopts myr-exposed [myr(e)] and -sequestered [myr(s)] states, as anticipated. Unexpectedly, the tertiary structures of the protein in both states are very similar, with the sequestered myristyl group occupying a cavity that requires only minor conformational adjustments for insertion. In addition, myristate exposure is coupled with trimerization, with the myristyl group sequestered in the monomer and exposed in the trimer ( K assoc = 2.5 ± 0.6 × 10 8 M –2 ). The equilibrium constant is shifted ≈20-fold toward the trimeric, myristate-exposed species in a Gag-like construct that includes the capsid domain, indicating that exposure is enhanced by Gag subdomains that promote self-association. Our findings indicate that the HIV-1 myristyl switch is regulated not by mechanically induced conformational changes, as observed for other myristyl switches, but instead by entropic modulation of a preexisting equilibrium.
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Cites
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Self-citation
Cited by
HIV-1 assembly, release and maturation
Freed, E. O. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3490 · Cited by 654
Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
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Self-citationThe structural biology of HIV assembly
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Plasma Membrane Is the Site of Productive HIV-1 Particle Assembly
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The Interferon Response Inhibits HIV Particle Production by Induction of TRIM22
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Metadata
- Authors
- Tang, C., Loeliger, E., Luncsford, P., Kinde, I., Beckett, D., & Summers, M. F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-12-29
- Volume
- 101
- Issue
- 2
- Pages
- 517-522
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2172285292
- Cited by
- 320
- References
- 12
- FWCI
- 4.64
- Type
- journal article
- Language
- en
- Open access
- green
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