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  4. Comparing Native Crystal Structures and AlphaFold2 Predicted Water-Soluble G Protein-Coupled Receptor QTY Variants

Comparing Native Crystal Structures and AlphaFold2 Predicted Water-Soluble G Protein-Coupled Receptor QTY Variants

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Author(s)
Skuhersky, Michael A.
•
Tao, Fei
•
Qing, Rui
•
Smorodina, Eva
•
Jin, David
•
Zhang, Shuguang
Date Issued
November 24, 2021
Publisher
Multidisciplinary Digital Publishing Institute
Citation
Life 11 (12): 1285 (2021)
Version
Final published version
Abstract
Accurate predictions of 3-dimensional protein structures by AlphaFold2 is a game-changer for biology, especially for structural biology. Here we present the studies of several native chemokine receptors including CCR5, CCR9, CXCR2 and CXCR4 determined by X-ray crystallography, and their water-soluble QTY counter parts predicted by AlphaFold2. In the native structures, there are hydrophobic amino acids leucine (L), isoleucine (I), valine (V) and phenylalanine (F) in the transmembrane helices. These hydrophobic amino acids are systematically replaced by hydrophilic amino acids glutamine (Q), threonine (T), and tyrosine (Y). Thus, the QTY variants become water-soluble. We also present the superimposed structures of native CCR10, CXCR5, CXCR7 and an olfactory receptor OR1D2 and their water-soluble QTY variants. Since the CryoEM structural determinations for the QTY variants of CCR10QTY and OR1D2QTY are in progress, it will be of interest to compare them when the structures become available. The superimposed structures show remarkable similarity within RMSD 1Å–2Å despite significant sequence differences (~26%–~33%). We also show the differences of hydrophobicity patches between the native GPCR and their QTY variants. Our study provides insight into the subtle differences between the hydrophobic helices and hydrophilic helices, and may further stimulate designs of water-soluble membrane proteins and other aggregated proteins.
MIT Department
Massachusetts Institute of Technology. Media Laboratory
Massachusetts Institute of Technology. Department of Brain and Cognitive Sciences
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Creative Commons Attribution
https://creativecommons.org/licenses/by/4.0/
Persistent DSpace Link
https://hdl.handle.net/1721.1/138236
DOI of Published Version
https://doi.org/10.3390/life11121285
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