Evidence map›Paper›PMID 34947816›Full record

ArticleLife (Basel, Switzerland)2021

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

Michael A Skuhersky, Fei Tao, Rui Qing, Eva Smorodina, David Jin, Shuguang Zhang

Open access · goldAbstract read
In one paragraph

Article in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  3. Design of a water-soluble CD20 antigen with computational epitope scaffolding.Protein science : a publication of the Protein Society · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 3 countries.

Michael A SkuherskyLaboratory of Molecular Architecture, Media Lab E15-391, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Fei TaoLaboratory of Molecular Architecture, Media Lab E15-391, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Rui QingLaboratory of Molecular Architecture, Media Lab E15-391, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Eva SmorodinaFaculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119991 Moscow, Russia.ORCID 0000-0002-5457-5163
David JinAvalon GloboCare Corp., Freehold, NJ 07728, USA.
Shuguang ZhangLaboratory of Molecular Architecture, Media Lab E15-391, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Shanghai Jiao Tong University · CNAvalon Pharma (United States) · USLomonosov Moscow State University · RUMassachusetts Institute of Technology · US

Funding

Avalon-GloboCare MITOSP6940423
6 · The paper itself

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 CCR10

Indexed as

chemokine receptorsmembrane protein designprotein structural predictionsQTY codewater-soluble GPCRs

Identifiers

PMID34947816
PMCPMC8704054
OpenAlexW3217332298

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.