2022Journal of VirologyOpen access

Insight into Viral Hijacking of CRL4 Ubiquitin Ligase through Structural Analysis of the pUL145-DDB1 Complex

Elizaveta T. Wick, Colton J. Treadway, Zhijun Li, Nathan I. Nicely, Zhizhong Ren, Albert S. Baldwin, Yue Xiong, Joseph S. Harrison, Nicholas G. Brown

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Abstract

creates a selective advantage for the virus. The DDB1-pUL145 peptide structure reveals that water-mediated interactions are critical to the higher affinity. Together, our data present an interesting example of how viral evolution can exploit a weakness in the ubiquitination machinery.

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What this paper is about

creates a selective advantage for the virus. The DDB1-pUL145 peptide structure reveals that water-mediated interactions are critical to the higher affinity. Together, our data present an interesting example of how viral evolution can exploit a weakness in the ubiquitination machinery.

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OpenAlex reports 6 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

creates a selective advantage for the virus. The DDB1-pUL145 peptide structure reveals that water-mediated interactions are critical to the higher affinity. Together, our data present an interesting example of how viral evolution can exploit a weakness in the ubiquitination machinery.

Key concepts: Cullin, Biology, DDB1, Ubiquitin ligase, Ubiquitin, Ubiquitin-Protein Ligases, DNA ligase, Cell biology

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