1MFS

DYNAMICAL BEHAVIOR OF THE HIV-1 NUCLEOCAPSID PROTEIN; NMR, 30 STRUCTURES

Summary for 1MFS

• Entry DOI: 10.2210/pdb1mfs/pdb
• Descriptor: HIV-1 NUCLEOCAPSID PROTEIN, ZINC ION (2 entities in total)
• Functional Keywords: nucleocapsid protein, dynamics, zinc knuckle, hiv-1, zinc binding, viral protein
• Biological source: Human immunodeficiency virus
• Cellular location: Gag-Pol polyprotein: Host cell membrane; Lipid-anchor. Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P35963
• Total number of polymer chains: 1
• Total formula weight: 6517.31

Authors

Summers, M.F.,Turner, B.G.,De Guzman, R.N.,Lee, B.M.,Tjandra, N. (deposition date: 1998-04-01, release date: 1998-06-17, Last modification date: 2024-05-01)

Primary citation

Lee, B.M.,De Guzman, R.N.,Turner, B.G.,Tjandra, N.,Summers, M.F.
Dynamical behavior of the HIV-1 nucleocapsid protein.
J.Mol.Biol., 279:633-649, 1998

PubMed 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 interactions, which involve the close approach of the side-chains of Phe16 and Trp37, are transitory. The solution behavior of NC may be best considered as a rapid equilibrium between conformations with weakly interacting and non-interacting knuckle domains. This inherent conformational flexibility may be functionally important, enabling adaptive binding of NC to different recognition elements within the HIV-1 psi-RNA packaging signal.

PubMed: 9641983
DOI: 10.1006/jmbi.1998.1766

Experimental method

SOLUTION NMR