Abstract
HIV-1 capsid protein (CA) encloses the viral RNA genome and forms a conical-shaped particle in the mature HIV-1 virion, with orderly capsid assembly and disassembly critically important for viral infectivity. The 231 residue CA is composed of two helical domains, connected by a short linker sequence. In solution, CA exhibits concentration dependent dimerization which is mediated by the C-terminal domain (CTD). Here, we present nearly complete (1)H, (15)N and (13)C assignments for the 20 kDa homodimeric CA-CTD, a prerequisite for structural characterization of the CA-CTD dimer.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Sequence
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Capsid Proteins / chemistry*
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Capsid Proteins / genetics
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Carbon Isotopes / chemistry
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HIV-1 / chemistry*
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Hydrogen / chemistry
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Models, Molecular
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Nitrogen Isotopes / chemistry
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Nuclear Magnetic Resonance, Biomolecular / methods
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Protein Multimerization
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Protein Structure, Secondary
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Protein Structure, Tertiary
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gag Gene Products, Human Immunodeficiency Virus / chemistry*
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gag Gene Products, Human Immunodeficiency Virus / genetics
Substances
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Capsid Proteins
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Carbon Isotopes
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Nitrogen Isotopes
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gag Gene Products, Human Immunodeficiency Virus
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Hydrogen