Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein.
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Summary
Alignment of the CA(146-231) dimer with the crystal structure of the capsid amino-terminal domain provides a model for the intact protein and extends models for assembly of the central conical core of HIV-1.
- Type
- article
- Published
- 1997-10-31
- Cited by
- 607
- References
- 46
- OpenAlex
- https://openalex.org/W2013652077
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:16821941
Keywords
Capsid, Dimer, Amino terminal, Crystallography, Chemistry
References
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- HIV-1 Gag protein associates with F-actin present in microfilaments.
- Structure of the Amino-Terminal Core Domain of the HIV-1 Capsid Protein
- Specific incorporation of cyclophilin A into HIV-1 virions
- A major retroviral core protein related to EPA and TIMP
- Protein structure comparison by alignment of distance matrices.
- Molecular recognition in the HIV-1 capsid/cyclophilin A complex.
- Structure of the actin-myosin complex and its implications for muscle contraction.
- Metal ion chaperone function of the soluble Cu(I) receptor Atx1.
- Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B.
- Crystal structure of dimeric HIV-1 capsid protein
- Distinct signals in human immunodeficiency virus type 1 Pr55 necessary for RNA binding and particle formation.
- Characterization of HIV‐1 p24 self‐association using analytical affinity chromatography
- Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid.
Cited by
- HIV-1 Gag: An Emerging Target for Antiretroviral Therapy
- Maturation inhibitors: a new therapeutic class targets the virus structure.
- The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle Assembly
- trans-Complementation Rescue of Cyclophilin A-Deficient Viruses Reveals that the Requirement for Cyclophilin A in Human Immunodeficiency Virus Type 1 Replication Is Independent of Its Isomerase Activity
- Intracellular Targeting of Gag Proteins of the Drosophila Telomeric Retrotransposons
- Investigation of N-terminal domain charged residues on the assembly and stability of HIV-1 CA.
- 3-O-(3′,3′-Dimethysuccinyl) Betulinic Acid Inhibits Maturation of the Human Immunodeficiency Virus Type 1 Gag Precursor Assembled In Vitro
- Quantitative Fluorescence Resonance Energy Transfer Microscopy Analysis of the Human Immunodeficiency Virus Type 1 Gag-Gag Interaction: Relative Contributions of the CA and NC Domains and Membrane Binding
- Structural changes in the SL5 and SL6 leader sequences of HIV-1 RNA following interactions with the viral mGag protein.
- Determination of the Structures of Symmetric Protein Oligomers from NMR Chemical Shifts and Residual Dipolar Couplings
- Reconstitution of selective HIV-1 RNA packaging in vitro by membrane-bound Gag assemblies
- Dynamic regulation of HIV-1 capsid interaction with the restriction factor TRIM5α identified by magic-angle spinning NMR and molecular dynamics simulations
- Hybrid vigor: hybrid methods in viral structure determination.
- Multimerization and membrane distribution of the Gag structural polyprotein during HIV-1 assembly
- Proteomic Investigation of the HIV Receptors CD4 and DC-Sign/CD209
- Cellular immunity driving HIV-1 evolution
- Determinants of HIV-1 Gag Localization to Uropods in Polarized T Cells and the Role Uropods Play in Virus Spread.
- Tubular Crystals and Helical Arrays: Structural Determination of HIV-1 Capsid Assemblies Using Iterative Helical Real-Space Reconstruction
- Targeting the Early Step of Building Block Organization in Viral Capsid Assembly.
- Rôle de la lysyl-ARNt synthétase mitochondriale humaine dans la réplication du VIH-1
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