2xgy | pdb_00002xgy

COMPLEX OF RABBIT ENDOGENOUS LENTIVIRUS (RELIK)CAPSID WITH CYCLOPHILIN A

spinqualitylabelsall models 2xgy, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xgy is a 2 chain structure with sequence from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Related: 1vbs, 1oca, 1mf8, 2cyh, 1cwb, 1vbt, 1cwl, 1m9e, 1cwc, 1cwo, 1cwi, 2x2c, 1rmh, 1cwj, 2rmb, 1m9c, 1cwa, 1cwf, 3cyh, 1m9y, 4cyh, 1m9f, 1cwh, 1bck, 1w8v, 1awr, 1nmk, 1mik, 1awv, 1m9d, 1awt, 2cpl, 1fgl, 2x2a, 1m9x, 1cwk, 1m63, 5cyh, 2x2d, 1ak4, 1aws, 2alf, 3cys, 1w8l, 2x25, 1w8m, 1awu, 2rma, 1cwm, 1awq, 2xgu Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural and functional analysis of prehistoric lentiviruses uncovers an ancient molecular interface.,Goldstone DC, Yap MW, Robertson LE, Haire LF, Taylor WR, Katzourakis A, Stoye JP, Taylor IA Cell Host Microbe. 2010 Sep 16;8(3):248-59. PMID:20833376 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cyclophilin Virus coat protein

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