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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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| Publicat a: | Protein Sci |
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| Autors principals: | , , , , , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
John Wiley & Sons, Inc.
2019
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| Matèries: | |
| Accés en línia: | 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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