2XGV

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

Summary for 2XGV

• Entry DOI: 10.2210/pdb2xgv/pdb
• Related: 2XGU 2XGY
• Descriptor: PSIV CAPSID N-TERMINAL DOMAIN (2 entities in total)
• Functional Keywords: retroviral capsid, viral protein
• Biological source: MICROCEBUS MURINUS (GREY MOUSE LEMUR)
• Total number of polymer chains: 1
• Total formula weight: 15993.89

Authors

Goldstone, D.C.,Robertson, L.E.,Haire, L.F.,Stoye, J.P.,Taylor, I.A. (deposition date: 2010-06-07, release date: 2010-09-22, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)