X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability

Author:

Gres Anna T.12,Kirby Karen A.13,KewalRamani Vineet N.4,Tanner John J.25,Pornillos Owen6,Sarafianos Stefan G.135

Affiliation:

1. Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO 65211, USA.

2. Department of Chemistry, University of Missouri, Columbia, MO 65211, USA.

3. Department of Molecular Microbiology and Immunology, University of Missouri School of Medicine, Columbia, MO 65211, USA.

4. Basic Research Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA.

5. Department of Biochemistry, University of Missouri, Columbia, MO 65211, USA.

6. Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.

Abstract

Retroviral capsids in their native form Capsid proteins of retroviruses form protective lattices around viral RNA molecules. The precise molecular details of how individual, full-length capsid proteins assemble to shield the viral genome; however, are not well understood. Obal et al. and Gres et al. now report high resolution crystal structures of the full length capsid proteins from Bovine Leukemia Virus and HIV-1, respectively. The two studies complement each other to reveal the dynamic nature of capsid protein assembly and of how individual capsid proteins interact in the lattice. The findings may have relevance for drug design. Science , this issue p. 95 ; see also p. 99

Funder

NIH

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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