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Author Henriquez, D.R.; Zhao, C.F.; Zheng, H.Y.; Arbildua, J.J.; Acevedo, M.L.; Roth, M.J.; Leon, O. pdf  doi
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  Title Crosslinking and mass spectrometry suggest that the isolated NTD domain dimer of Moloney murine leukemia virus integrase adopts a parallel arrangement in solution Type
  Year 2013 Publication Bmc Structural Biology Abbreviated Journal BMC Struct. Biol.  
  Volume 13 Issue Pages 12 pp  
  Keywords  
  Abstract Background: Retroviral integrases (INs) catalyze the integration of viral DNA in the chromosomal DNA of the infected cell. This reaction requires the multimerization of IN to coordinate a nucleophilic attack of the 3' ends of viral DNA at two staggered phosphodiester bonds on the recipient DNA. Several models indicate that a tetramer of IN would be required for two-end concerted integration. Complementation assays have shown that the N-terminal domain (NTD) of integrase is essential for concerted integration, contributing to the formation of a multimer through protein-protein interaction. The isolated NTD of Mo-MLV integrase behave as a dimer in solution however the structure of the dimer in solution is not known. Results: In this work, crosslinking and mass spectrometry were used to identify regions involved in the dimerization of the isolated Mo-MLV NTD. The distances between the crosslinked lysines within the monomer are in agreement with the structure of the NTD monomer found in 3NNQ. The intermolecular crosslinked peptides corresponding to Lys 20-Lys 31, Lys 24-Lys 24 and Lys 68-Lys 88 were identified. The 3D coordinates of 3NNQ were used to derive a theoretical structure of the NTD dimer with the suite 3D-Dock, based on shape and electrostatics complementarity, and filtered with the distance restraints determined in the crosslinking experiments. Conclusions: The crosslinking results are consistent with the monomeric structure of NTD in 3NNQ, but for the dimer, in our model both polypeptides are oriented in parallel with each other and the contacting areas between the monomers would involve the interactions between helices 1 and helices 3 and 4.  
  Address [Henriquez, Daniel R.; Acevedo, Monica L.; Leon, Oscar] Univ Chile, Fac Med, Programa Virol ICBM, Santiago 7, Chile, Email: oleon@med.uchile.cl  
  Corporate Author Thesis  
  Publisher Biomed Central Ltd Place of Publication Editor  
  Language English Summary Language Original Title  
  Series Editor Series Title Abbreviated Series Title  
  Series Volume Series Issue Edition (up)  
  ISSN 1472-6807 ISBN Medium  
  Area Expedition Conference  
  Notes WOS:000322963600001 Approved  
  Call Number UAI @ eduardo.moreno @ Serial 466  
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