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2XGV

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

2XGV の概要
エントリーDOI10.2210/pdb2xgv/pdb
関連するPDBエントリー2XGU 2XGY
分子名称PSIV CAPSID N-TERMINAL DOMAIN (2 entities in total)
機能のキーワードretroviral capsid, viral protein
由来する生物種MICROCEBUS MURINUS (GREY MOUSE LEMUR)
タンパク質・核酸の鎖数1
化学式量合計15993.89
構造登録者
Goldstone, D.C.,Robertson, L.E.,Haire, L.F.,Stoye, J.P.,Taylor, I.A. (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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 2xgv
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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