ArticleProtein science : a publication of the Protein Society2002
Nef of HIV-1 interacts directly with calcium-bound calmodulin.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 47 citations in OpenAlex.
- Quantitative and amino acid sequence analysis of soluble HIV-1 Vpu and calmodulin interactions.Protein science : a publication of the Protein Society · 2026Article
- A novel antiviral strategy by disrupting the equilibrium of virus-host calcium homeostasis.Current opinion in virology · 2026Review
- Profiling HIV1-host protein-protein interaction networks in patient-derived exosome proteins: impact on pathophysiology and innate immune pathways.Virology journal · 2025Article
- A Non-Canonical Calmodulin Target Motif Comprising a Polybasic Region and Lipidated Terminal Residue Regulates Localization.International journal of molecular sciences · 2020Review
- Differential Contribution of HIV-1 Subtypes B and C to Neurological Disorders: Mechanisms and Possible Treatments.AIDS reviews · 2019Review
- The transcriptomics of an experimentally evolved plant-virus interaction.Scientific reports · 2016Article
- Article
- Structural and Biophysical Characterization of the Interactions between Calmodulin and the Pleckstrin Homology Domain of Akt.The Journal of biological chemistry · 2015Article
- Calmodulin and PI(3,4,5)P₃ cooperatively bind to the Itk pleckstrin homology domain to promote efficient calcium signaling and IL-17A production.Science signaling · 2014Article
- Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein.The Journal of biological chemistry · 2014Article
- Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.Frontiers in microbiology · 2012Article
- NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein.The Journal of biological chemistry · 2011Article
- Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure.The Journal of biological chemistry · 2010Article
- HIV and SIV induce alterations in CNS CaMKII expression and activation: a potential mechanism for cognitive impairment.The American journal of pathology · 2010Article
- Exogenous Nef is an inhibitor of Mycobacterium tuberculosis-induced tumor necrosis factor-alpha production and macrophage apoptosis.The Journal of biological chemistry · 2010Article
- Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous system.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2010Review
- Calcium-dependent association of calmodulin with the rubella virus nonstructural protease domain.The Journal of biological chemistry · 2010Article
- Myristoylation of the small envelope protein of porcine reproductive and respiratory syndrome virus is non-essential for virus infectivity but promotes its growth.Virus research · 2010Article
- N-myristoylated proteins, key components in intracellular signal transduction systems enabling rapid and flexible cell responses.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2010Review
- Viral calciomics: interplays between Ca2+ and virus.Cell calcium · 2009Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It was recently found that the myristoyl group of CAP-23/NAP-22, a neuron-specific protein kinase C substrate, is essential for the interaction between the protein and Ca(2+)-bound calmodulin (Ca(2+)/CaM). Based on the N-terminal amino acid sequence alignment of CAP-23/NAP-22 and other myristoylated proteins, including the Nef protein from human immunodeficiency virus (HIV), we proposed a new hypothesis that the protein myristoylation plays important roles in protein-calmodulin interactions. To investigate the possibility of direct interaction between Nef and calmodulin, we performed structural studies of Ca(2+)/CaM in the presence of a myristoylated peptide corresponding to the N-terminal region of Nef. The dissociation constant between Ca(2+)/CaM and the myristoylated Nef peptide was determined to be 13.7 nM by fluorescence spectroscopy analyses. The NMR experiments indicated that the chemical shifts of some residues on and around the hydrophobic clefts of Ca(2+)/CaM changed markedly in the Ca(2+)/CaM-Nef peptide complex with the molar ratio of 1:2. Correspondingly, the radius of gyration determined by the small angle X-ray scattering measurements is 2-3 A smaller that of Ca(2+)/CaM alone. These results demonstrate clearly that Nef interacts directly with Ca(2+)/CaM.
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