3H4E
X-ray Structure of Hexameric HIV-1 CA
3H4E の概要
エントリーDOI | 10.2210/pdb3h4e/pdb |
関連するPDBエントリー | 3gv2 3h47 |
分子名称 | Capsid protein p24 (1 entity in total) |
機能のキーワード | capsid protein, hexamer, engineered disulfide bonds, viral protein |
由来する生物種 | Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE) (HIV-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 | 12 |
化学式量合計 | 305535.25 |
構造登録者 | |
主引用文献 | Pornillos, O.,Ganser-Pornillos, B.K.,Kelly, B.N.,Hua, Y.,Whitby, F.G.,Stout, C.D.,Sundquist, W.I.,Hill, C.P.,Yeager, M. X-ray structures of the hexameric building block of the HIV capsid. Cell(Cambridge,Mass.), 137:1282-1292, 2009 Cited by PubMed Abstract: The mature capsids of HIV and other retroviruses organize and package the viral genome and its associated enzymes for delivery into host cells. The HIV capsid is a fullerene cone: a variably curved, closed shell composed of approximately 250 hexamers and exactly 12 pentamers of the viral CA protein. We devised methods for isolating soluble, assembly-competent CA hexamers and derived four crystallographically independent models that define the structure of this capsid assembly unit at atomic resolution. A ring of six CA N-terminal domains form an apparently rigid core, surrounded by an outer ring of C-terminal domains. Mobility of the outer ring appears to be an underlying mechanism for generating the variably curved lattice in authentic capsids. Hexamer-stabilizing interfaces are highly hydrated, and this property may be key to the formation of quasi-equivalent interactions within hexamers and pentamers. The structures also clarify the molecular basis for capsid assembly inhibition and should facilitate structure-based drug design strategies. PubMed: 19523676DOI: 10.1016/j.cell.2009.04.063 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.704 Å) |
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