|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6vsi' size='340' side='right'caption='[[6vsi]], [[Resolution|resolution]] 1.87Å' scene=''> | | <StructureSection load='6vsi' size='340' side='right'caption='[[6vsi]], [[Resolution|resolution]] 1.87Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6vsi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/B11220 B11220]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VSI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VSI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vsi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_auris Candida auris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VSI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.87Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CJJ09_002997 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=498019 B11220])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=6vsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vsi OCA], [https://pdbe.org/6vsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vsi RCSB], [https://www.ebi.ac.uk/pdbsum/6vsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vsi ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vsi OCA], [http://pdbe.org/6vsi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vsi RCSB], [http://www.ebi.ac.uk/pdbsum/6vsi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vsi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A2H1A4Z6_CANAR A0A2H1A4Z6_CANAR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 19: |
| | </div> | | </div> |
| | <div class="pdbe-citations 6vsi" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6vsi" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[FKBP 3D structures|FKBP 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: B11220]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidylprolyl isomerase]]
| + | [[Category: Hernandez G]] |
| - | [[Category: Hernandez, G]] | + | [[Category: LeMaster D]] |
| - | [[Category: LeMaster, D]] | + | [[Category: Li H]] |
| - | [[Category: Li, H]] | + | [[Category: Li Z]] |
| - | [[Category: Li, Z]] | + | |
| - | [[Category: C. auri]]
| + | |
| - | [[Category: Fkbp12]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Pathogenesis]]
| + | |
| Structural highlights
Function
A0A2H1A4Z6_CANAR
Publication Abstract from PubMed
International concern over the recent emergence of Candida auris infections reflects not only its comparative ease of transmission and substantial mortality but the increasing level of resistance observed to all three major classes of antifungal drugs. Diminution in virulence has been reported for a wide range of fungal pathogens when the FK506-binding protein FKBP12 binds to that immunosuppressant drug and the binary complex then inhibits the fungal calcineurin signaling pathway. Structure-based drug design efforts have described modifications of FK506 which modestly reduce virulence for a number of fungal pathogens while also lessening the side effect of suppressing the tissue immunity response in the patient. To aid in such studies, we report the crystal structure of Candida auris FKBP12. As physiological relevance has been proposed for transient homodimerization interactions of distantly related fungal FKBP12 proteins, we report the solution NMR characterization of the homodimerization interactions of the FKBP12 proteins from both Candida auris and Candida glabrata.
Crystal structure and transient dimerization for the FKBP12 protein from the pathogenic fungus Candida auris.,Bashir Q, Li Z, Li H, LeMaster DM, Hernandez G Biochem Biophys Res Commun. 2020 Mar 14. pii: S0006-291X(20)30544-1. doi:, 10.1016/j.bbrc.2020.03.059. PMID:32184021[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bashir Q, Li Z, Li H, LeMaster DM, Hernandez G. Crystal structure and transient dimerization for the FKBP12 protein from the pathogenic fungus Candida auris. Biochem Biophys Res Commun. 2020 Mar 14. pii: S0006-291X(20)30544-1. doi:, 10.1016/j.bbrc.2020.03.059. PMID:32184021 doi:http://dx.doi.org/10.1016/j.bbrc.2020.03.059
|
