2XGY

Complex of Rabbit Endogenous Lentivirus (RELIK)Capsid with Cyclophilin A

Summary for 2XGY

• Entry DOI: 10.2210/pdb2xgy/pdb
• Related: 1AK4 1AWQ 1AWR 1AWS 1AWT 1AWU 1AWV 1BCK 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1FGL 1M63 1M9C 1M9D 1M9E 1M9F 1M9X 1M9Y 1MF8 1MIK 1NMK 1OCA 1RMH 1VBS 1VBT 1W8L 1W8M 1W8V 2ALF 2CPL 2CYH 2RMA 2RMB 2X25 2X2A 2X2C 2X2D 2XGU 3CYH 3CYS 4CYH 5CYH
• Descriptor: RELIK CAPSID N-TERMINAL DOMAIN, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A, GLYCEROL, ... (4 entities in total)
• Functional Keywords: viral protein-isomerase complex, retroviral capsid, endogenous, viral protein/isomerase
• Biological source: ORYCTOLAGUS CUNICULUS (RABBIT); More
• Cellular location: Cytoplasm: P62937
• Total number of polymer chains: 2
• Total formula weight: 35517.36

Authors

Goldstone, D.C.,Robertson, L.E.,Haire, L.F.,Stoye, J.P.,Taylor, I.A. (deposition date: 2010-06-08, 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 (1.8 Å)