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Science 31 October 1997:
Vol. 278. no. 5339, pp. 849 - 853
DOI: 10.1126/science.278.5339.849
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Reports

Structure of the Carboxyl-Terminal Dimerization Domain of the HIV-1 Capsid Protein

Theresa R. Gamble, * Sanghee Yoo, * Felix F. Vajdos, Uta K. von Schwedler, David K. Worthylake, Hui Wang, John P. McCutcheon, Wesley I. Sundquist, dagger Christopher P. Hill dagger

The carboxyl-terminal domain, residues 146 to 231, of the human immunodeficiency virus-1 (HIV-1) capsid protein [CA(146-231)] is required for capsid dimerization and viral assembly. This domain contains a stretch of 20 residues, called the major homology region (MHR), which is conserved across retroviruses and is essential for viral assembly, maturation, and infectivity. The crystal structures of CA(146-231) and CA(151-231) reveal that the globular domain is composed of four helices and an extended amino-terminal strand. CA(146-231) dimerizes through parallel packing of helix 2 across a dyad. The MHR is distinct from the dimer interface and instead forms an intricate hydrogen-bonding network that interconnects strand 1 and helices 1 and 2. Alignment of the CA(146-231) dimer with the crystal structure of the capsid amino-terminal domain provides a model for the intact protein and extends models for assembly of the central conical core of HIV-1.

Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.
*   These authors contributed equally to this report.

dagger    To whom correspondence should be addressed.

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M. Dettenhofer and X.-F. Yu (1999)
J. Virol. 73, 4696-4704
   Abstract »    Full Text »
Structural similarities between influenza virus matrix protein M1 and human immunodeficiency virus matrix and capsid proteins: an evolutionary link between negative-stranded RNA viruses and retroviruses.
A Harris, B Sha, and M Luo (1999)
J. Gen. Virol. 80, 863-869
   Abstract »
Interaction of the Human Immunodeficiency Virus Type 1 Nucleocapsid with Actin.
B. Liu, R. Dai, C.-J. Tian, L. Dawson, R. Gorelick, and X.-F. Yu (1999)
J. Virol. 73, 2901-2908
   Abstract »    Full Text »
Maturation-induced Conformational Changes of HIV-1 Capsid Protein and Identification of Two High Affinity Sites for Cyclophilins in the C-terminal Domain.
M. M. Endrich, P. Gehrig, and H. Gehring (1999)
J. Biol. Chem. 274, 5326-5332
   Abstract »    Full Text »    PDF »
Virus Maturation by Budding.
H. Garoff, R. Hewson, and D.-J. E. Opstelten (1998)
Microbiol. Mol. Biol. Rev. 62, 1171-1190
   Abstract »    Full Text »    PDF »
The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle Assembly.
A. Borsetti, A. Ohagen, and H. G. Gottlinger (1998)
J. Virol. 72, 9313-9317
   Abstract »    Full Text »    PDF »
Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: Implications for retroviral assembly mechanisms.
M. Yeager, E. M. Wilson-Kubalek, S. G. Weiner, P. O. Brown, and A. Rein (1998)
PNAS 95, 7299-7304
   Abstract »    Full Text »    PDF »
Organization of HIV-1 Capsid Proteins on a Lipid Monolayer.
E. Barklis, J. McDermott, S. Wilkens, S. Fuller, and D. Thompson (1998)
J. Biol. Chem. 273, 7177-7180
   Abstract »    Full Text »    PDF »
A Putative alpha -Helical Structure Which Overlaps the Capsid-p2 Boundary in the Human Immunodeficiency Virus Type 1 Gag Precursor Is Crucial for Viral Particle Assembly.
M. A. Accola, S. Hoglund, and H. G. Gottlinger (1998)
J. Virol. 72, 2072-2078
   Abstract »    Full Text »    PDF »


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