ArticleThe Journal of biological chemistry2011
NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 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
- Subtype Differences in the Interaction of HIV-1 Matrix with Calmodulin: Implications for Biological Functions.Biomolecules · 2021Article
- High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulin.Magnetic resonance (Gottingen, Germany) · 2021Article
- How HIV-1 Gag Manipulates Its Host Cell Proteins: A Focus on Interactors of the Nucleocapsid Domain.Viruses · 2020Review
- Structural and biophysical characterizations of HIV-1 matrix trimer binding to lipid nanodiscs shed light on virus assembly.The Journal of biological chemistry · 2019Article
- Calmodulin Enhances Cryptochrome Binding to INAD inFrontiers in molecular neuroscience · 2018Article
- Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.Structure (London, England : 1993) · 2017Article
- The Interplay between Calmodulin and Membrane Interactions with the Pleckstrin Homology Domain of Akt.The Journal of biological chemistry · 2017Article
- Article
- Effect of Glu12-His89 Interaction on Dynamic Structures in HIV-1 p17 Matrix Protein Elucidated by NMR.PloS one · 2016Article
- Structural and Biophysical Characterization of the Interactions between Calmodulin and the Pleckstrin Homology Domain of Akt.The Journal of biological chemistry · 2015Article
- Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein.The Journal of biological chemistry · 2014Article
- Role of Gag and lipids during HIV-1 assembly in CD4(+) T cells and macrophages.Frontiers in microbiology · 2014Review
- Structural and biophysical characterization of the interactions between the death domain of Fas receptor and calmodulin.The Journal of biological chemistry · 2013Article
- Molecular mechanism of arenavirus assembly and budding.Viruses · 2012Review
- Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release.Biophysical journal · 2012Article
- Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.Frontiers in microbiology · 2012Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Subcellular distribution of Calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1)-infected cells is distinct from that observed in uninfected cells. CaM has been shown to interact and co-localize with the HIV-1 Gag protein in infected cells. However, the precise molecular mechanism of this interaction is not known. Binding of Gag to CaM is dependent on calcium and is mediated by the N-terminal-myristoylated matrix (myr(+)MA) domain. We have recently shown that CaM binding induces a conformational change in the MA protein, triggering exposure of the myristate group. To unravel the molecular mechanism of CaM-MA interaction and to identify the minimal CaM binding domain of MA, we devised multiple approaches utilizing NMR, biochemical, and biophysical methods. Short peptides derived from the MA protein have been examined. Our data revealed that whereas peptides spanning residues 11-28 (MA-(11-28)) and 31-46 (MA-(31-46)) appear to bind preferentially to the C-terminal lobe of CaM, a peptide comprising residues 11-46 (MA-(11-46)) appears to engage both domains of CaM. Limited proteolysis data conducted on the MA-CaM complex yielded a MA peptide (residues 8-43) that is protected by CaM and resistant to proteolysis. MA-(8-43) binds to CaM with a very high affinity (dissociation constant = 25 nm) and in a manner that is similar to that observed for the full-length MA protein. The present findings provide new insights on how MA interacts with CaM that may ultimately help in identification of the functional role of CaM-Gag interactions in the HIV replication cycle.
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