5NA2

Crystal structure of the full-length Feline Immunodeficiency Virus capsid protein unveils original features

5NA2 の概要

• エントリーDOI: 10.2210/pdb5na2/pdb
• 分子名称: Capsid protein (p24), GLYCEROL (3 entities in total)
• 機能のキーワード: fiv, capsid, p24, ca, feline immunodeficiency virus, viral protein
• 由来する生物種: Feline immunodeficiency virus (isolate Petaluma) (FIV)
• 細胞内の位置: Matrix protein p15: Virion . Capsid protein p24: Virion . Nucleocapsid protein p13: Virion : P16087
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47824.63

構造登録者

Folio, C.,Sierra, N.,Dujardin, M.,Alvarez, G.,Guillon, C. (登録日: 2017-02-27, 公開日: 2017-11-15, 最終更新日: 2024-11-20)

主引用文献

Folio, C.,Sierra, N.,Dujardin, M.,Alvarez, G.,Guillon, C.
Crystal Structure of the Full-Length Feline Immunodeficiency Virus Capsid Protein Shows an N-Terminal beta-Hairpin in the Absence of N-Terminal Proline.
Viruses, 9:-, 2017

PubMed Abstract: Feline immunodeficiency virus (FIV) is a member of the Retroviridae family. It is the causative agent of an acquired immunodeficiency syndrome (AIDS) in cats and wild felines. Its capsid protein (CA) drives the assembly of the viral particle, which is a critical step in the viral replication cycle. Here, the first atomic structure of full-length FIV CA to 1.67 Å resolution is determined. The crystallized protein exhibits an original tetrameric assembly, composed of dimers which are stabilized by an intermolecular disulfide bridge induced by the crystallogenesis conditions. The FIV CA displays a standard α-helical CA topology with two domains, separated by a linker shorter than other retroviral CAs. The β-hairpin motif at its amino terminal end, which interacts with nucleotides in HIV-1, is unusually long in FIV CA. Interestingly, this functional β-motif is formed in this construct in the absence of the conserved N-terminal proline. The FIV CA exhibits a Arg-Pro bond in the CypA-binding loop, which is absent in known structures of lentiviral CAs. This structure represents the first tri-dimensional structure of a functional, full-length FIV CA.

PubMed: 29120364
DOI: 10.3390/v9110335

実験手法

X-RAY DIFFRACTION (1.67 Å)