Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code Article Swipe
YOU?
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· 2024
· Open Access
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· DOI: https://doi.org/10.1038/s41467-024-48513-9
Membrane proteins are critical to biological processes and central to life sciences and modern medicine. However, membrane proteins are notoriously challenging to study, mainly owing to difficulties dictated by their highly hydrophobic nature. Previously, we reported QTY code, which is a simple method for designing water-soluble membrane proteins. Here, we apply QTY code to a transmembrane receptor, histidine kinase CpxA, to render it completely water-soluble. The designed CpxA QTY exhibits expected biophysical properties and highly preserved native molecular function, including the activities of (i) autokinase, (ii) phosphotransferase, (iii) phosphatase, and (iv) signaling receptor, involving a water-solubilized transmembrane domain. We probe the principles underlying the balance of structural stability and activity in the water-solubilized transmembrane domain. Computational approaches suggest that an extensive and dynamic hydrogen-bond network introduced by QTY code and its flexibility may play an important role. Our successful functional preservation further substantiates the robustness and comprehensiveness of QTY code.
Related Topics
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s41467-024-48513-9
- https://www.nature.com/articles/s41467-024-48513-9.pdf
- OA Status
- gold
- Cited By
- 8
- References
- 70
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4399500106
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W4399500106Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1038/s41467-024-48513-9Digital Object Identifier
- Title
-
Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY codeWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2024Year of publication
- Publication date
-
2024-06-10Full publication date if available
- Authors
-
Mengke Li, Hongzhi Tang, Rui Qing, Yanze Wang, Jiongqin Liu, Rui Wang, Shan Lyu, Lina Ma, Ping Xu, Shuguang Zhang, Fei TaoList of authors in order
- Landing page
-
https://doi.org/10.1038/s41467-024-48513-9Publisher landing page
- PDF URL
-
https://www.nature.com/articles/s41467-024-48513-9.pdfDirect link to full text PDF
- Open access
-
YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
-
https://www.nature.com/articles/s41467-024-48513-9.pdfDirect OA link when available
- Concepts
-
Transmembrane protein, Function (biology), Code (set theory), Receptor, Kinase, Computational biology, Cell biology, Chemistry, Biology, Computer science, Biochemistry, Programming language, Set (abstract data type)Top concepts (fields/topics) attached by OpenAlex
- Cited by
-
8Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 5, 2024: 3Per-year citation counts (last 5 years)
- References (count)
-
70Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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