2c9l | pdb_00002c9l

Structure of the Epstein-Barr virus ZEBRA protein

spinqualitylabelsall models 2c9l, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c9l is a 4 chain structure with sequence from Ebvg. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1zsd, 2axf, 2axg, 2c9n Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Epstein-Barr virus (EBV) causes infectious mononucleosis and is linked to several human malignancies. EBV has a biphasic infection cycle consisting of a latent and a lytic, replicative phase. The switch from latent to lytic infection is triggered by the EBV immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1). We present the crystal structure of ZEBRA's DNA binding domain bound to an EBV lytic gene promoter element. ZEBRA exhibits a variant of the basic-region leucine zipper (bZIP) fold in which a C-terminal moiety stabilizes the coiled coil involved in dimer formation. The structure provides insights into ZEBRA's broad target site specificity, preferential activation of specific EBV promoters in their methylated state, ability to dimerize despite lacking a leucine zipper motif, and failure to heterodimerize with cellular bZIP proteins. The structure will allow for the design of new therapeutic agents that block activation of the EBV lytic cycle. Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein.,Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Muller CW Mol Cell. 2006 Feb 17;21(4):565-72. PMID:16483937 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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