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.
Jung
Jinwon
J
Department of Structural Biology and Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Byeon
In-Ja L
IJ
Ahn
Jinwoo
J
Concel
Jason
J
Gronenborn
Angela M
AM
D000595:Amino Acid Sequence; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics; D002247:Carbon Isotopes / Q000737:chemistry; D015497:HIV-1 / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry; D008958:Models, Molecular; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D054301:gag Gene Products, Human Immunodeficiency Virus / Q000737:chemistry* / Q000235:genetics
D036022:Capsid Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D054301:gag Gene Products, Human Immunodeficiency Virus; D006859:Hydrogen