Structural similarity between the p17 matrix protein of HIV-1 and interferon-γ

Stephen Matthews, Paul Barlow, Jonathan Boyd, Geoff Barton, Robert Russell, Helen Mills, Mark Cunningham, Nicola Meyers, Nigel Burns, Nigel Clark, Susan Kingsman, Alan Kingsman, Iain Campbell

Research output: Contribution to journalArticlepeer-review

130 Citations (Scopus)


THE human immunodeficiency virus (HIV) matrix protein, p17, forms the outer shell of the core of the virus, lining the inner surface of the viral membrane1-4. The protein has several key functions. It orchestrates viral assembly via targeting signals that direct the gag precursor polyprotein, p55, to the host cell membrane1,5-7 and it interacts with the transmembrane protein, gp41, to retain the env-encoded proteins in the virus8. In addition, pi7 contains a nuclear localization signal that directs the preintegration complex to the nucleus of infected cells9. This permits the virus to infect productively non-dividing cells, a distinguishing feature of HIV and other lentiviruses. We have determined the solution structure of p17 by nuclear magnetic resonance (NMR) with a root-mean square deviation for the backbone of the well-defined regions of 0.9 Å. It consists of four helices connected by short loops and an irregular, mixed β-sheet which provides a positively charged surface for interaction with the inner layer of the membrane. The helical topology is unusual; the Brookhaven protein database contains only one similar structure, that of the immune modulator interferon-γ.

Original languageEnglish
Pages (from-to)666-668
Number of pages3
Issue number6491
Publication statusPublished - 25 Aug 1994

ASJC Scopus subject areas

  • General


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