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(New page: 200px<br /><applet load="2fav" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fav, resolution 1.800Å" /> '''Crystal structure o...)
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Revision as of 08:20, 21 November 2007
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Crystal structure of SARS macro domain in complex with ADP-ribose at 1.8 A resolution
Overview
Macro domains constitute a protein module family found associated with, specific histones and proteins involved in chromatin metabolism. In, addition, a small number of animal RNA viruses, such as corona- and, toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for, which, however, structural and functional information is extremely, limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus, (SARS-CoV). The crystal structure of the SARS-CoV macro domain was, determined at 1.8-Angstroms resolution in complex with ADP-ribose., Information derived from structural, mutational, and sequence analyses, suggests a close phylogenetic and, most probably, functional relationship, between viral and cellular macro domain homologs. The data revealed that, viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase, activities (which were previously proposed to be their biologically, relevant function) but bind efficiently free and poly(ADP-ribose), polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results, suggest to further evaluate the role of viral macro domains in host, response to viral infection.
About this Structure
2FAV is a Single protein structure of sequence from Human sars coronavirus with APR as ligand. Full crystallographic information is available from OCA.
Reference
Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains., Egloff MP, Malet H, Putics A, Heinonen M, Dutartre H, Frangeul A, Gruez A, Campanacci V, Cambillau C, Ziebuhr J, Ahola T, Canard B, J Virol. 2006 Sep;80(17):8493-502. PMID:16912299
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