ArticleThe Journal of biological chemistry2014
Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 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
- The soluble state of the HIV-1 Vpu protein forms a complex with CaProtein science : a publication of the Protein Society · 2026Article
- Binding by calmodulin is coupled to transient unfolding of the third FF domain of Prp40A.Protein science : a publication of the Protein Society · 2023Article
- Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Subtype Differences in the Interaction of HIV-1 Matrix with Calmodulin: Implications for Biological Functions.Biomolecules · 2021Article
- Screening for the Proteins That Can Interact with Grouper Nervous Necrosis Virus Capsid Protein.Viruses · 2020Article
- Differences and commonalities in plasma membrane recruitment of the two morphogenetically distinct retroviruses HIV-1 and MMTV.The Journal of biological chemistry · 2020Article
- HIV-1 Virus Interactions With Host Proteins: Interaction of the N-terminal Domain of the HIV-1 Capsid Protein With Human Calmodulin.Natural product communications · 2019Article
- A Mechanism of Calmodulin Modulation of the Human Cardiac Sodium Channel.Structure (London, England : 1993) · 2018Article
- Structural characterization of the catalytic γ and regulatory β subunits of phosphorylase kinase in the context of the hexadecameric enzyme complex.Protein science : a publication of the Protein Society · 2018Article
- Effect of Glu12-His89 Interaction on Dynamic Structures in HIV-1 p17 Matrix Protein Elucidated by NMR.PloS one · 2016Article
- Improving HIV proteome annotation: new features of BioAfrica HIV Proteomics Resource.Database : the journal of biological databases and curation · 2016Article
- Article
- 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
- Role of Gag and lipids during HIV-1 assembly in CD4(+) T cells and macrophages.Frontiers in microbiology · 2014Review
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Authors and funding
3 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 co-localizes and interacts with the HIV-1 Gag protein in the cytosol of infected cells. Although it has been shown that binding of Gag to CaM is mediated by the matrix (MA) domain, the structural details of this interaction are not known. We have recently shown that binding of CaM to MA induces a conformational change that triggers myristate exposure, and that the CaM-binding domain of MA is confined to a region spanning residues 8-43 (MA-(8-43)). Here, we present the NMR structure of CaM bound to MA-(8-43). Our data revealed that MA-(8-43), which contains a novel CaM-binding motif, binds to CaM in an antiparallel mode with the N-terminal helix (α1) anchored to the CaM C-terminal lobe, and the C-terminal helix (α2) of MA-(8-43) bound to the N-terminal lobe of CaM. The CaM protein preserves a semiextended conformation. Binding of MA-(8-43) to CaM is mediated by numerous hydrophobic interactions and stabilized by favorable electrostatic contacts. Our structural data are consistent with the findings that CaM induces unfolding of the MA protein to have access to helices α1 and α2. It is noteworthy that several MA residues involved in CaM binding have been previously implicated in membrane binding, envelope incorporation, and particle production. The present findings may ultimately help in identification of the functional role of CaM in HIV-1 replication.
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