Journal
CHEMPHYSCHEM
Volume 22, Issue 14, Pages 1505-1517Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cphc.202100187
Keywords
NMR spectroscopy; protein structures; pseudocontact shift; residual dipolar coupling; ubiquitin
Funding
- JSPS KAKENHI [16H04752]
- AMED-SENTAN [JP16hm0102016]
- JST-CREST [JPMJCR1762]
- Institute for Protein Research, Osaka University [CR-20-02]
- China Scholarship council (CSC)
- Grants-in-Aid for Scientific Research [16H04752] Funding Source: KAKEN
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This study utilized paramagnetic NMR spectroscopy to investigate the conformational space of linear diubiquitin, revealing that the molecule prefers to sample particular regions of conformational space. By combining these findings with data on charge-reversal derivatives, structural insights into the binding events of linear diubiquitin were obtained.
Linear polyubiquitin chains regulate diverse signaling proteins, in which the chains adopt various conformations to recognize different target proteins. Thus, the structural plasticity of the chains plays an important role in controlling the binding events. Herein, paramagnetic NMR spectroscopy is employed to explore the conformational space sampled by linear diubiquitin, a minimal unit of linear polyubiquitin, in its free state. Rigorous analysis of the data suggests that, regarding the relative positions of the ubiquitin units, particular regions of conformational space are preferentially sampled by the molecule. By combining these results with further data collected for charge-reversal derivatives of linear diubiquitin, structural insights into the factors underlying the binding events of linear diubiquitin are obtained.
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