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| | <StructureSection load='6mdh' size='340' side='right'caption='[[6mdh]], [[Resolution|resolution]] 1.37Å' scene=''> | | <StructureSection load='6mdh' size='340' side='right'caption='[[6mdh]], [[Resolution|resolution]] 1.37Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mdh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/David's_myotis David's myotis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MDH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MDH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mdh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myotis_davidii Myotis davidii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MDH FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MDA_GLEAN10007532 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=225400 David's myotis])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mdh OCA], [http://pdbe.org/6mdh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mdh RCSB], [http://www.ebi.ac.uk/pdbsum/6mdh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mdh ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mdh OCA], [https://pdbe.org/6mdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mdh RCSB], [https://www.ebi.ac.uk/pdbsum/6mdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mdh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/L5LC70_MYODS L5LC70_MYODS] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6mdh" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6mdh" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[Journal:Acta Cryst D:S2059798318015322|Journal:Acta Cryst D:S2059798318015322]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: David's myotis]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Daczkowski, C M]] | + | [[Category: Myotis davidii]] |
| - | [[Category: Dzimianski, J V]] | + | [[Category: Daczkowski CM]] |
| - | [[Category: Goodwin, O Y]] | + | [[Category: Dzimianski JV]] |
| - | [[Category: Langley, C A]] | + | [[Category: Goodwin OY]] |
| - | [[Category: Pegan, S D]] | + | [[Category: Langley CA]] |
| - | [[Category: Innate immune response]] | + | [[Category: Pegan SD]] |
| - | [[Category: Interferon]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Ubiquitin-like]]
| + | |
| Structural highlights
Function
L5LC70_MYODS
Publication Abstract from PubMed
Bats have long been observed to be the hosts and the origin of numerous human diseases. Bats, like all mammals, rely on a number of innate immune mechanisms to combat invading pathogens, including the interferon type I, II and III responses. Ubiquitin-like interferon-stimulated gene product 15 (ISG15) is a key modulator of these interferon responses. Within these pathways, ISG15 can serve to stabilize host proteins modulating innate immune responses and act as a cytokine. Post-translational modifications of viral proteins introduced by ISG15 have also been observed to directly affect the function of numerous viral proteins. Unlike ubiquitin, which is virtually identical across all animals, comparison of ISG15s across species reveals that they are relatively divergent, with sequence identity dropping to as low as approximately 58% among mammals. In addition to serving as an obstacle to the zoonotic transmission of influenza, these ISG15 species-species differences have also long been shown to have an impact on the function of viral deISGylases. Recently, the structure of the first nonhuman ISG15, originating from mouse, suggested that the structures of human ISG15 may not be reflective of other species. Here, the structure of ISG15 from the bat species Myotis davidii solved to 1.37 A resolution is reported. Comparison of this ISG15 structure with those from 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 the papain-like deISGylase from Severe acute respiratory syndrome coronavirus as a probe, the biochemical importance of this motif in ISG15-protein engagements was illuminated.
Structure of interferon-stimulated gene product 15 (ISG15) from the bat species Myotis davidii and the impact of interdomain ISG15 interactions on viral protein engagement.,Langley C, Goodwin O, Dzimianski JV, Daczkowski CM, Pegan SD Acta Crystallogr D Struct Biol. 2019 Jan 1;75(Pt 1):21-31. doi:, 10.1107/S2059798318015322. Epub 2019 Jan 4. PMID:30644842[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Langley C, Goodwin O, Dzimianski JV, Daczkowski CM, Pegan SD. Structure of interferon-stimulated gene product 15 (ISG15) from the bat species Myotis davidii and the impact of interdomain ISG15 interactions on viral protein engagement. Acta Crystallogr D Struct Biol. 2019 Jan 1;75(Pt 1):21-31. doi:, 10.1107/S2059798318015322. Epub 2019 Jan 4. PMID:30644842 doi:http://dx.doi.org/10.1107/S2059798318015322
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