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Springer (part of Springer Nature), Biomolecular NMR Assignments, 1(4), p. 21-23

DOI: 10.1007/s12104-009-9198-9

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

Journal article published in 2009 by Jinwon Jung, In-Ja L. Byeon, Jinwoo Ahn, Jason Concel, Angela M. Gronenborn ORCID
This paper is available in a repository.
This paper is available in a repository.

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Data provided by SHERPA/RoMEO

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 1H, 15N and 13C assignments for the 20 kDa homodimeric CA–CTD, a prerequisite for structural characterization of the CA–CTD dimer.