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-Structure paper
タイトル | Structural basis for dimerization quality control. |
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ジャーナル・号・ページ | Nature, Vol. 586, Issue 7829, Page 452-456, Year 2020 |
掲載日 | 2020年8月19日 |
![]() | Elijah L Mena / Predrag Jevtić / Basil J Greber / Christine L Gee / Brandon G Lew / David Akopian / Eva Nogales / John Kuriyan / Michael Rape / ![]() |
PubMed 要旨 | Most quality control pathways target misfolded proteins to prevent toxic aggregation and neurodegeneration. Dimerization quality control further improves proteostasis by eliminating complexes of ...Most quality control pathways target misfolded proteins to prevent toxic aggregation and neurodegeneration. Dimerization quality control further improves proteostasis by eliminating complexes of aberrant composition, but how it detects incorrect subunits remains unknown. Here we provide structural insight into target selection by SCF-FBXL17, a dimerization-quality-control E3 ligase that ubiquitylates and helps to degrade inactive heterodimers of BTB proteins while sparing functional homodimers. We find that SCF-FBXL17 disrupts aberrant BTB dimers that fail to stabilize an intermolecular β-sheet around a highly divergent β-strand of the BTB domain. Complex dissociation allows SCF-FBXL17 to wrap around a single BTB domain, resulting in robust ubiquitylation. SCF-FBXL17 therefore probes both shape and complementarity of BTB domains, a mechanism that is well suited to establish quality control of complex composition for recurrent interaction modules. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 2.2 - 8.5 Å |
構造データ | EMDB-21617, PDB-6wcq: ![]() PDB-6w66: ![]() PDB-6w67: ![]() PDB-6w68: ![]() PDB-6w69: |
化合物 | ![]() ChemComp-HOH: |
由来 |
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![]() | LIGASE/SIGNALING PROTEIN / ![]() ![]() ![]() ![]() ![]() ![]() ![]() |