2XGU

Structure of the N-terminal domain of capsid protein from Rabbit Endogenous Lentivirus (RELIK)

2XGU の概要

• エントリーDOI: 10.2210/pdb2xgu/pdb
• 関連するPDBエントリー: 2XGV 2XGY
• 分子名称: RELIK CAPSID N-TERMINAL DOMAIN, ACETATE ION (3 entities in total)
• 機能のキーワード: viral protein, retroviral capsid
• 由来する生物種: ORYCTOLAGUS CUNICULUS (RABBIT)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33082.68

構造登録者

Goldstone, D.C.,Taylor, I.A.,Robertson, L.E.,Haire, L.F.,Stoye, J.P. (登録日: 2010-06-07, 公開日: 2010-09-22, 最終更新日: 2024-05-08)

主引用文献

Goldstone, D.C.,Yap, M.W.,Robertson, L.E.,Haire, L.F.,Taylor, W.R.,Katzourakis, A.,Stoye, J.P.,Taylor, I.A.
Structural and Functional Analysis of Prehistoric Lentiviruses Uncovers an Ancient Molecular Interface.
Cell Host Microbe, 8:248-, 2010

PubMed Abstract: Lentiviruses are widespread in a variety of vertebrates, often associated with chronic disease states. However, until the recent discovery of the prehistoric endogenous lentiviruses in rabbits (RELIK) and lemurs (PSIV), it was thought that lentiviruses had no capacity for germline integration and were only spread horizontally in an exogenous fashion. The existence of RELIK and PSIV refuted these ideas, revealing lentiviruses to be present in a range of mammals, capable of germline integration, and far more ancient than previously thought. Using Gag sequences reconstructed from the remnants of these prehistoric lentiviruses, we have produced chimeric lentiviruses capable of infecting nondividing cells and determined structures of capsid domains from PSIV and RELIK. We show that the structures from these diverse viruses are highly similar, containing features found in modern-day lentiviruses, including a functional cyclophilin-binding loop. Together, these data provide evidence for an ancient capsid-cyclophilin interaction preserved throughout lentiviral evolution.

PubMed: 20833376
DOI: 10.1016/J.CHOM.2010.08.006

実験手法

X-RAY DIFFRACTION (1.502 Å)