1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein.

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.