1BAJ

HIV-1 CAPSID PROTEIN C-TERMINAL FRAGMENT PLUS GAG P2 DOMAIN

Summary for 1BAJ

• Entry DOI: 10.2210/pdb1baj/pdb
• Descriptor: GAG POLYPROTEIN (2 entities in total)
• Functional Keywords: capsid, hiv-1 assembly protein, viral protein
• Biological source: Human immunodeficiency virus 1
• Cellular location: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497
• Total number of polymer chains: 1
• Total formula weight: 11107.77

Authors

Worthylake, D.K.,Wang, H.,Yoo, S.,Sundquist, W.I.,Hill, C.P. (deposition date: 1998-04-17, release date: 1998-10-14, Last modification date: 2024-10-30)

Primary citation

Worthylake, D.K.,Wang, H.,Yoo, S.,Sundquist, W.I.,Hill, C.P.
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution.
Acta Crystallogr.,Sect.D, 55:85-92, 1999

PubMed Abstract: The human immunodeficiency virus type I (HIV-1) capsid protein is initially synthesized as the central domain of the Gag polyprotein, and is subsequently proteolytically processed into a discrete 231-amino-acid protein that forms the distinctive conical core of the mature virus. The crystal structures of two proteins that span the C-terminal domain of the capsid are reported here: one encompassing residues 146-231 (CA146-231) and the other extending to include the 14-residue p2 domain of Gag (CA146-p2). The isomorphous CA146-231 and CA146-p2 structures were determined by molecular replacement and have been refined at 2.6 A resolution to R factors of 22.3 and 20.7% (Rfree = 28.1 and 27.5%), respectively. The ordered domains comprise residues 148-219 for CA146-231 and 148-218 for CA146-p2, and their refined structures are essentially identical. The proteins are composed of a 310 helix followed by an extended strand and four alpha-helices. A crystallographic twofold generates a dimer that is stabilized by parallel packing of an alpha-helix 2 across the dimer interface and by packing of the 310 helix into a groove created by alpha-helices 2 and 3 of the partner molecule. CA146-231 and CA146-p2 dimerize with the full affinity of the intact capsid protein, and their structures therefore reveal the essential dimer interface of the HIV-1 capsid.

PubMed: 10089398
DOI: 10.1107/S0907444998007689

Experimental method

X-RAY DIFFRACTION (2.6 Å)