2HMX

HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX PROTEIN

「1HMX」から置き換えられました

2HMX の概要

• エントリーDOI: 10.2210/pdb2hmx/pdb
• 分子名称: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX PROTEIN (1 entity in total)
• 機能のキーワード: hiv-1 p17, hiv-1 ma, matrix protein
• 由来する生物種: Human immunodeficiency virus 1
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15003.96

構造登録者

Massiah, M.A.,Starich, M.R.,Paschall, C.,Christensen, A.M.,Sundquist, W.I.,Summers, M.F. (登録日: 1995-09-22, 公開日: 1996-01-29, 最終更新日: 2024-05-29)

主引用文献

Massiah, M.A.,Starich, M.R.,Paschall, C.,Summers, M.F.,Christensen, A.M.,Sundquist, W.I.
Three-dimensional structure of the human immunodeficiency virus type 1 matrix protein.
J.Mol.Biol., 244:198-223, 1994

PubMed Abstract: The HIV-1 matrix protein forms an icosahedral shell associated with the inner membrane of the mature virus. Genetic analyses have indicated that the protein performs important functions throughout the viral life-cycle, including anchoring the transmembrane envelope protein on the surface of the virus, assisting in viral penetration, transporting the proviral integration complex across the nuclear envelope, and localizing the assembling virion to the cell membrane. We now report the three-dimensional structure of recombinant HIV-1 matrix protein, determined at high resolution by nuclear magnetic resonance (NMR) methods. The HIV-1 matrix protein is the first retroviral matrix protein to be characterized structurally and only the fourth HIV-1 protein of known structure. NMR signal assignments required recently developed triple-resonance (1H, 13C, 15N) NMR methodologies because signals for 91% of 132 assigned H alpha protons and 74% of the 129 assignable backbone amide protons resonate within chemical shift ranges of 0.8 p.p.m. and 1 p.p.m., respectively. A total of 636 nuclear Overhauser effect-derived distance restraints were employed for distance geometry-based structure calculations, affording an average of 13.0 NMR-derived distance restraints per residue for the experimentally constrained amino acids. An ensemble of 25 refined distance geometry structures with penalties (sum of the squares of the distance violations) of 0.32 A2 or less and individual distance violations under 0.06 A was generated; best-fit superposition of ordered backbone heavy atoms relative to mean atom positions afforded root-mean-square deviations of 0.50 (+/- 0.08) A. The folded HIV-1 matrix protein structure is composed of five alpha-helices, a short 3(10) helical stretch, and a three-strand mixed beta-sheet. Helices I to III and the 3(10) helix pack about a central helix (IV) to form a compact globular domain that is capped by the beta-sheet. The C-terminal helix (helix V) projects away from the beta-sheet to expose carboxyl-terminal residues essential for early steps in the HIV-1 infectious cycle. Basic residues implicated in membrane binding and nuclear localization functions cluster about an extruded cationic loop that connects beta-strands 1 and 2. The structure suggests that both membrane binding and nuclear localization may be mediated by complex tertiary structures rather than simple linear determinants.

PubMed: 7966331
DOI: 10.1006/jmbi.1994.1719

実験手法

SOLUTION NMR