Journal:Acta Cryst D:S2059798318015322

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Recently, the structure of the first non-human ISG15 originating from mouse suggested that human structures of ISG15s may not be reflective of other species. Here, the <scene name='80/800124/Cv/2'>structure of ISG15</scene> from the bat species ''Myotis davidii'' solved to 1.37 Å is reported ([[6mdh]]). Comparison of this ISG15 structure with those of human and mouse not only underscores the structural impact of ISG15 species-species differences, but also highlights a conserved hydrophobic motif formed between the two domains of ISG15. Using papain-like deISGylase from the severe acute respiratory coronavirus as a probe, the biochemical importance of this interface and its species-species variances on ISG15-protein engagements was illuminated.
Recently, the structure of the first non-human ISG15 originating from mouse suggested that human structures of ISG15s may not be reflective of other species. Here, the <scene name='80/800124/Cv/2'>structure of ISG15</scene> from the bat species ''Myotis davidii'' solved to 1.37 Å is reported ([[6mdh]]). Comparison of this ISG15 structure with those of human and mouse not only underscores the structural impact of ISG15 species-species differences, but also highlights a conserved hydrophobic motif formed between the two domains of ISG15. Using papain-like deISGylase from the severe acute respiratory coronavirus as a probe, the biochemical importance of this interface and its species-species variances on ISG15-protein engagements was illuminated.
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<scene name='80/800124/Cv/5'>Overlay of ISG15s from bat, mouse, and human</scene>. Structures of hISG15 (green), mISG15 (purple), and bISG15 (blue) are superimposed using the least squared fit of residues comprising the C-terminal domain on each respective protein. <scene name='80/800124/Cv/6'>TextToBeDisplayed</scene>.
<b>References</b><br>
<b>References</b><br>

Revision as of 12:12, 13 November 2018

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