5o9l: Difference between revisions
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New page: '''Unreleased structure''' The entry 5o9l is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
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==Crystal structure of human Histamine-Releasing Factor (HRF/TCTP)== | |||
<StructureSection load='5o9l' size='340' side='right'caption='[[5o9l]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<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='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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TCTP_HUMAN TCTP_HUMAN] Involved in calcium binding and microtubule stabilization. | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:29216544</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5o9l" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Davies AM]] | |||
[[Category: Dore KA]] | |||
[[Category: Gould HJ]] | |||
[[Category: Kashiwakura J]] | |||
[[Category: Kawakami T]] | |||
[[Category: McDonnell JM]] | |||
[[Category: Sutton BJ]] | |||
Latest revision as of 09:37, 6 December 2023
Crystal structure of human Histamine-Releasing Factor (HRF/TCTP)
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