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| Structure of the amino-terminal core domain of the HIV-1 capsid protein |
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| Author(s): Gitti RK, Lee BM, Walker J, Summers MF, Yoo S, Sundquist WI |
| Source: SCIENCE Volume: 273 Issue: 5272 Pages: 231-235 Published: JUL 12 1996 |
| Times Cited: 255 References: 103 |
| Abstract: The three-dimensional structure of the amino-terminal core domain (residues 1 through 151) of the human immunodeficiency virus-type 1 (HIV-1) capsid protein has been solved by multidimensional heteronuclear magnetic resonance spectroscopy. The structure is unlike those of previously characterized viral coat proteins and is composed of seven alpha helices, two beta hairpins, and an exposed partially ordered loop. The domain is shaped like an arrowhead, with the beta hairpins and loop exposed at the trailing edge and the carboxyl-terminal helix projecting from the tip. The proline residue Pro(1) forms a salt bridge with a conserved, buried aspartate residue (Asp(51)), which suggests that the amino terminus of the protein rearranges upon proteolytic maturation. The binding site for cyclophilin A, a cellular rotamase that is packaged into the HIV-1 virion, is located on the exposed loop and encompasses the essential proline residue Pro(90). In the free monomeric domain, Pro(90) adopts kinetically trapped cis and trans conformations, raising the possibility that cyclophilin A catalyzes interconversion of the cis- and trans-Pro(90) loop structures. |
| Document Type: Review |
| Language: English |
| Reprint Address: Gitti, RK (reprint author), UNIV MARYLAND BALTIMORE CTY, HOWARD HUGHES MED INST, BALTIMORE, MD 21228 USA |
Addresses:
1. UNIV MARYLAND BALTIMORE CTY, DEPT CHEM & BIOCHEM, BALTIMORE, MD 21228 USA
2. UNIV UTAH, DEPT BIOCHEM, SALT LAKE CITY, UT 84132 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: UW787 |
| ISSN: 0036-8075 |
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