Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code

Mengke Li, Hongzhi Tang, Rui Qing, Yanze Wang, Jiongqin Liu, Rui Wang, Shan Lyu, Lina Ma, Ping Xu (), Shuguang Zhang () and Fei Tao ()
Additional contact information
Mengke Li: Shanghai Jiao Tong University
Hongzhi Tang: Shanghai Jiao Tong University
Rui Qing: Shanghai Jiao Tong University
Yanze Wang: Massachusetts Institute of Technology
Jiongqin Liu: Shanghai Jiao Tong University
Rui Wang: Shanghai Jiao Tong University
Shan Lyu: Shanghai Jiao Tong University
Lina Ma: Shanghai Jiao Tong University
Ping Xu: Shanghai Jiao Tong University
Shuguang Zhang: Massachusetts Institute of Technology
Fei Tao: Shanghai Jiao Tong University

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: Abstract 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 CpxAQTY 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.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-48513-9 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-48513-9

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-48513-9

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().