Evidence map›Paper›PMID 39089252›Full record

ArticleCell2024

Molecular mechanism of distinct chemokine engagement and functional divergence of the human Duffy antigen receptor.

Shirsha Saha, Basavraj Khanppnavar, Jagannath Maharana, Heeryung Kim, Carlo Marion C Carino, Carole Daly, Shane Houston, Saloni Sharma, Nashrah Zaidi, Annu Dalal and 12 more

Abstract read
In one paragraph

Article in Cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

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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

22 authors.

Shirsha SahaDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Basavraj KhanppnavarLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland; Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Jagannath MaharanaDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Heeryung KimSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Carlo Marion C CarinoGraduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai, Miyagi 980-8578, Japan.
Carole DalyWellcome-Wolfson Institute for Experimental Medicine, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast, UK.
Shane HoustonWellcome-Wolfson Institute for Experimental Medicine, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast, UK.
Saloni SharmaDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Nashrah ZaidiDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Annu DalalDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Sudha MishraDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Manisankar GangulyDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Divyanshu TiwariDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India.
Poonam KumariDivision of Neuroscience and Ageing Biology, CSIR-Central Drug Research Institute, Lucknow, India.
Gagan Deep JhinganValerian Chem Pvt. Ltd., Vproteomics, New Delhi 110049, India.
Prem N YadavDivision of Neuroscience and Ageing Biology, CSIR-Central Drug Research Institute, Lucknow, India.
Bianca PlouffeWellcome-Wolfson Institute for Experimental Medicine, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast, UK.
Asuka InoueGraduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai, Miyagi 980-8578, Japan.
Ka Young ChungSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Ramanuj BanerjeeDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India. Electronic address: ramanujb@iitk.ac.in.
Volodymyr M KorkhovLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland; Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland. Electronic address: volodymyr.korkhov@psi.ch.
Arun K ShuklaDepartment of Biological Sciences and Bioengineering, Indian Institute of Technology Kanpur, Kanpur 208016, India. Electronic address: arshukla@iitk.ac.in.

Funding

DBT-Wellcome Trust India Alliance IA/S/20/1/504916
6 · The paper itself

Abstract

The Duffy antigen receptor is a seven-transmembrane (7TM) protein expressed primarily at the surface of red blood cells and displays strikingly promiscuous binding to multiple inflammatory and homeostatic chemokines. It serves as the basis of the Duffy blood group system in humans and also acts as the primary attachment site for malarial parasite Plasmodium vivax and pore-forming toxins secreted by Staphylococcus aureus. Here, we comprehensively profile transducer coupling of this receptor, discover potential non-canonical signaling pathways, and determine the cryoelectron microscopy (cryo-EM) structure in complex with the chemokine CCL7. The structure reveals a distinct binding mode of chemokines, as reflected by relatively superficial binding and a partially formed orthosteric binding pocket. We also observe a dramatic shortening of TM5 and 6 on the intracellular side, which precludes the formation of the docking site for canonical signal transducers, thereby providing a possible explanation for the distinct pharmacological and functional phenotype of this receptor.

Indexed as

Cryoelectron MicroscopyDuffy Blood-Group SystemReceptors, Cell SurfaceBinding SitesChemokinesHumansProtein BindingSignal TransductionACKR1 protein, humanChemokinesDuffy Blood-Group SystemReceptors, Cell SurfaceACKR1atypical chemokine receptorscellular signalingchemokine receptorscryogenic-electron microscopyDuffy antigen receptorG protein-coupled receptors

Identifiers

PMID39089252
PMCPMC11349380

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.