7vu5
From Proteopedia
Structure of the transmembrane domain of the CD28 dimer
Structural highlights
FunctionCD28_HUMAN Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival. Publication Abstract from PubMedCD28 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Homo sapiens | Large Structures | Cao R | Ouyang B | Wen M | Wu H
