Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Mapping of immunogenic and protein-interacting regions at the surface of the seven-bladed β-propeller domain of the HIV-1 cellular interactor EED | Virology Journal BioMed Central Research Mapping of immunogenic and protein-interacting regions at the surface of the seven-bladed P-propeller domain of the HIV-I cellular interactor EED Dina Rakotobe1 Sébastien Violot1 2 Saw See Hong1 Patrice Gouet2 and Pierre Boulanger 1 3 Open Access Address 1Laboratoire de Virologie Pathologie Humaine Université Lyon I CNRS FRE-3011 Faculté de Médecine Laennec 7 rue Guillaume Paradin 69372 Lyon Cedex 08 France 2Laboratoire de BioCristallographie IBCP Instititut Fédératif de Recherche IFR128 BioSciences Lyon-Gerland 7 passage du Vercors 69367 Lyon Cedex 07 France and 3Laboratoire de Virologie Médicale Centre de Biologie Pathologie du Pôle Est Hospices Civils de Lyon 59 Boulevard Pinel 69677 Bron Cedex France Email Dina Rakotobe - dinaraktb@ Sébastien Violot - Saw See Hong - Patrice Pierre Boulanger - Corresponding author Published 27 February 2008 Received 22 January 2008 Accepted 27 February 2008 Virology journal 2008 5 32 doi 1743-422X-5-32 This article is available from http content 5 1 32 2008 Rakotobe et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background The human EED protein a member of the superfamily of Polycomb group proteins is involved in multiple cellular protein complexes. Its C-terminal domain which is common to the four EED isoforms contains seven repeats of a canonical WD-40 motif. EED is an interactor of three HIV-1 proteins matrix MA integrase IN and Nef. An antiviral activity has been found to be associated with isoforms EED3 and EED4 at the late stage of HIV-1 replication due to a negative effect on .