Dynamical behavior of the HIV-1 nucleocapsid protein

Journal of Molecular Biology
B M LeeM F Summers

Abstract

The HIV-1 nucleocapsid protein (NC) contains two CCHC-type zinc knuckle domains that are essential for genome recognition, packaging and infectivity. The solution structure of the protein has been determined independently by three groups. Although the structures of the individual zinc knuckle domains are similar, two of the studies indicated that the knuckles behave as independently folded, non-interacting domains connected by a flexible tether, whereas one study revealed the presence of interknuckle NOE cross-peaks, which were interpreted in terms of a more compact structure in which the knuckles are in close proximity. We have collected multidimensional NMR data for the recombinant, isotopically labeled HIV-1 NC protein, and confirmed the presence of weak interknuckle NOEs. However, the NOE data are not consistent with a single protein conformation. 15N NMR relaxation studies reveal that the two zinc knuckle domains possess different effective rotational correlation times, indicating that the knuckles are not tumbling as a single globular domain. In addition, the 1H NMR chemical shifts of isolated zinc knuckle peptides are very similar to those of the intact protein. The combined results indicate that the interknuckle interac...Continue Reading

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Citations

Nov 25, 1998·Protein Science : a Publication of the Protein Society·Y GaoD P Giedroc
Aug 3, 2005·Nature Reviews. Microbiology·Victoria D'Souza, Michael F Summers
Aug 25, 2000·AIDS Research and Human Retroviruses·H De RocquignyB P Roques
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Apr 29, 1999·Proceedings of the National Academy of Sciences of the United States of America·S DruillennecM C Fournié-Zaluski
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Apr 11, 2017·ChemMedChem·Mrinmoy SahaDaniel H Appella
Jan 8, 1999·Journal of Molecular Biology·B G Turner, M F Summers
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Dec 16, 2010·RNA Biology·Delphine Muriaux, Jean-Luc Darlix
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