3DIK

Pseudo-atomic model of the HIV-1 CA hexameric lattice

3DIK の概要

• エントリーDOI: 10.2210/pdb3dik/pdb
• EMDBエントリー: 1529
• 分子名称: Capsid protein p24 (1 entity in total)
• 機能のキーワード: mature retroviral capsid, fullerene cone, hexamer, aids, aspartyl protease, capsid maturation, capsid protein, dna integration, dna recombination, dna-directed dna polymerase, endonuclease, hydrolase, lipoprotein, magnesium, metal-binding, multifunctional enzyme, myristate, nuclease, nucleotidyltransferase, nucleus, phosphoprotein, protease, rna-binding, rna-directed dna polymerase, transferase, viral nucleoprotein, virion, zinc-finger, viral protein
• 由来する生物種: Human immunodeficiency virus type 1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24498.08

構造登録者

Ganser-Pornillos, B.K.,Cheng, A.,Yeager, M. (登録日: 2008-06-20, 公開日: 2008-09-16, 最終更新日: 2024-02-21)

主引用文献

Ganser-Pornillos, B.K.,Cheng, A.,Yeager, M.
Structure of full-length HIV-1 CA: a model for the mature capsid lattice
Cell(Cambridge,Mass.), 131:70-79, 2007

PubMed Abstract: The capsids of mature retroviruses perform the essential function of organizing the viral genome for efficient replication. These capsids are modeled as fullerene structures composed of closed hexameric arrays of the viral CA protein, but a high-resolution structure of the lattice has remained elusive. A three-dimensional map of two-dimensional crystals of the R18L mutant of HIV-1 CA was derived by electron cryocrystallography. The docking of high-resolution domain structures into the map yielded the first unambiguous model for full-length HIV-1 CA. Three important protein-protein assembly interfaces are required for capsid formation. Each CA hexamer is composed of an inner ring of six N-terminal domains and an outer ring of C-terminal domains that form dimeric linkers connecting neighboring hexamers. Interactions between the two domains of CA further stabilize the hexamer and provide a structural explanation for the mechanism of action of known HIV-1 assembly inhibitors.

PubMed: 17923088
DOI: 10.1016/j.cell.2007.08.018

実験手法

ELECTRON CRYSTALLOGRAPHY (9 Å)