Dimerization of a ubiquitin variant leads to high affinity interactions with a ubiquitin interacting motif

We previously described structural and functional characterization of the first ubiquitin variant (UbV), UbV.v27.1, engineered by phage display to bind with high affinity to a specific ubiquitin interacting motif (UIM). We identified two substitutions relative to ubiquitin (Gly10Val/His68Tyr) that w...

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Detalhes bibliográficos
Publicado no:Protein Sci
Main Authors: Manczyk, Noah, Veggiani, Gianluca, Gish, Gerald D., Yates, Bradley P., Ernst, Andreas, Sidhu, Sachdev S., Sicheri, Frank
Formato: Artigo
Idioma:Inglês
Publicado em: John Wiley & Sons, Inc. 2019
Assuntos:
Accelerated Communication
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC6459996/
https://ncbi.nlm.nih.gov/pubmed/30793400
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.3593
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