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| | <StructureSection load='5o9l' size='340' side='right'caption='[[5o9l]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='5o9l' size='340' side='right'caption='[[5o9l]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5o9l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O9L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5O9L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5o9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O9L FirstGlance]. <br> |
| - | </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=5o9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9l OCA], [http://pdbe.org/5o9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o9l RCSB], [http://www.ebi.ac.uk/pdbsum/5o9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9l ProSAT]</span></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]] 1.75Å</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=5o9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9l OCA], [https://pdbe.org/5o9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o9l RCSB], [https://www.ebi.ac.uk/pdbsum/5o9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TCTP_HUMAN TCTP_HUMAN]] Involved in calcium binding and microtubule stabilization. | + | [https://www.uniprot.org/uniprot/TCTP_HUMAN TCTP_HUMAN] Involved in calcium binding and microtubule stabilization. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davies, A M]] | + | [[Category: Davies AM]] |
| - | [[Category: Dore, K A]] | + | [[Category: Dore KA]] |
| - | [[Category: Gould, H J]] | + | [[Category: Gould HJ]] |
| - | [[Category: Kashiwakura, J]] | + | [[Category: Kashiwakura J]] |
| - | [[Category: Kawakami, T]] | + | [[Category: Kawakami T]] |
| - | [[Category: McDonnell, J M]] | + | [[Category: McDonnell JM]] |
| - | [[Category: Sutton, B J]] | + | [[Category: Sutton BJ]] |
| - | [[Category: Allergy]]
| + | |
| - | [[Category: Fortilin]]
| + | |
| - | [[Category: Histamine releasing factor]]
| + | |
| - | [[Category: Hrf]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Immunoglobulin e]]
| + | |
| - | [[Category: P21]]
| + | |
| - | [[Category: P23]]
| + | |
| - | [[Category: Tctp]]
| + | |
| Structural highlights
Function
TCTP_HUMAN Involved in calcium binding and microtubule stabilization.
Publication Abstract from PubMed
In allergic disease, mast cell activation is conventionally triggered by allergen-mediated cross-linking of receptor-bound IgE on the cell surface. In addition to its diverse range of intracellular roles in apoptosis, cell proliferation and cancer, Histamine-Releasing Factor (HRF) also activates mast cells and basophils. A subset of IgE antibodies bind HRF through their Fab regions, and two IgE binding sites on HRF have been mapped. HRF can form dimers, and a disulphide-linked dimer is critical for activity. The current model for the activity of HRF in mast cell activation involves cross-linking of receptor-bound IgE by dimeric HRF, mediated by HRF/Fab interactions. HRF crystal and solution structures have provided little insight into either the formation of disulphide-linked HRF dimers or the ability of HRF to activate mast cells. We report the first crystal structure of murine HRF (mHRF) to 4.0A resolution, revealing a conserved fold. We also solved the structure of human HRF (hHRF) in two new crystal forms, one at the highest resolution (1.4A) yet reported. The high resolution hHRF structure reveals a disulphide-linked dimer, in which the two molecules are closely associated, and provides a model for the role of both human and murine HRF in mast cell activation.
Crystal structures of murine and human Histamine-Releasing Factor (HRF/TCTP) and a model for HRF dimerisation in mast cell activation.,Dore KA, Kashiwakura JI, McDonnell JM, Gould HJ, Kawakami T, Sutton BJ, Davies AM Mol Immunol. 2018 Jan;93:216-222. doi: 10.1016/j.molimm.2017.11.022. Epub 2017, Dec 5. PMID:29216544[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dore KA, Kashiwakura JI, McDonnell JM, Gould HJ, Kawakami T, Sutton BJ, Davies AM. Crystal structures of murine and human Histamine-Releasing Factor (HRF/TCTP) and a model for HRF dimerisation in mast cell activation. Mol Immunol. 2018 Jan;93:216-222. doi: 10.1016/j.molimm.2017.11.022. Epub 2017, Dec 5. PMID:29216544 doi:http://dx.doi.org/10.1016/j.molimm.2017.11.022
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