7vu5

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(New page: '''Unreleased structure''' The entry 7vu5 is ON HOLD Authors: Wu, H., Cao, R., Wen, M., Ouyang, B. Description: Structure of the transmembrane domain of the CD28 dimer [[Category: Unre...)
Current revision (11:21, 14 June 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 7vu5 is ON HOLD
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==Structure of the transmembrane domain of the CD28 dimer==
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<StructureSection load='7vu5' size='340' side='right'caption='[[7vu5]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7vu5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VU5 FirstGlance]. <br>
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</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=7vu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vu5 OCA], [https://pdbe.org/7vu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vu5 RCSB], [https://www.ebi.ac.uk/pdbsum/7vu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vu5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CD28_HUMAN CD28_HUMAN] Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CD28 has a crucial role in regulating immune responses by enhancing T cell activation and differentiation. Recent studies have shown that the transmembrane helix (TMH) of CD28 mediates receptor assembly and activity, but a structural characterization of TMH is still lacking. Here, we determined the dimeric helix-helix packing of CD28-TMH using nuclear magnetic resonance (NMR) technology. Unexpectedly, wild-type CD28-TMH alone forms stable tetramers in lipid bicelles instead of dimers. The NMR structure of the CD28-TMH C165F mutant reveals that a GxxxA motif, which is highly conserved in many dimeric assemblies, is located at the dimerization interface. Mutating G160 and A164 can disrupt the transmembrane helix assembly and reduces CD28 enhancement in cells. In contrast, a previously proposed YxxxxT motif does not affect the dimerization of full-length CD28, but it does affect CD28 activity. These results imply that the transmembrane domain of CD28 regulates the signaling transduction in a complicated manner.
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Authors: Wu, H., Cao, R., Wen, M., Ouyang, B.
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Structural characterization of a dimerization interface in the CD28 transmembrane domain.,Wu H, Cao R, Wen M, Xue H, OuYang B Structure. 2022 Jun 2;30(6):803-812.e5. doi: 10.1016/j.str.2022.03.004. Epub 2022, Apr 8. PMID:35397202<ref>PMID:35397202</ref>
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Description: Structure of the transmembrane domain of the CD28 dimer
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Ouyang, B]]
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<div class="pdbe-citations 7vu5" style="background-color:#fffaf0;"></div>
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[[Category: Wu, H]]
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== References ==
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[[Category: Cao, R]]
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<references/>
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[[Category: Wen, M]]
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Cao R]]
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[[Category: Ouyang B]]
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[[Category: Wen M]]
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[[Category: Wu H]]

Current revision

Structure of the transmembrane domain of the CD28 dimer

PDB ID 7vu5

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