Evidence map›Paper›PMID 29143165›Full record

ArticleJournal of biomolecular NMR2017

Structure of monomeric Interleukin-8 and its interactions with the N-terminal Binding Site-I of CXCR1 by solution NMR spectroscopy.

Sabrina Berkamp, Sang Ho Park, Anna A De Angelis, Francesca M Marassi, Stanley J Opella

Open access · greenAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-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

23 citing papers in PubMed, 31 citations in OpenAlex.

  1. SpyCEP dismantles neutrophil immunity via disorder-driven chemokine remodeling and GAG targeting.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

5 authors at 2 institutions in 1 country.

Sabrina BerkampDepartment of Chemistry and Biochemistry, University of California, San Diego La Jolla, San Diego, CA, 92093-0307, USA.
Sang Ho ParkDepartment of Chemistry and Biochemistry, University of California, San Diego La Jolla, San Diego, CA, 92093-0307, USA.
Anna A De AngelisDepartment of Chemistry and Biochemistry, University of California, San Diego La Jolla, San Diego, CA, 92093-0307, USA.
Francesca M MarassiSanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, San Diego, CA, 92037, USA.
Stanley J OpellaDepartment of Chemistry and Biochemistry, University of California, San Diego La Jolla, San Diego, CA, 92093-0307, USA. sopella@ucsd.edu.
University of California, San Diego · USDiscovery Institute · US

Funding

RESOURCE FOR SOLID STATE NMR OF PROTEINSP41EB002031 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2018
$16.3M
Membrane Protein Effectors of Pathogen Interactions With HostR35GM118186 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Francesca M Marassi · 2016 to 2026
$8.5M
Structure, Dynamics, and Functions of the Viroporins Vpu from HIV and p7 from HCVR01GM066978 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2016
$3.5M
Structures, Dynamics, and Functions of Membrane ProteinsR35GM122501 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2017 to 2021
$2.5M
NIBIB NIH HHS P41 EB002031NIGMS NIH HHS R01 GM066978NIGMS NIH HHS R35 GM118186NIGMS NIH HHS R35 GM122501NIH HHS P41EB002031NIH HHS R35GM118186NIH HHS R35GM122501NIH HHS RO1GM066978
6 · The paper itself

Abstract

The structure of monomeric human chemokine IL-8 (residues 1-66) was determined in aqueous solution by NMR spectroscopy. The structure of the monomer is similar to that of each subunit in the dimeric full-length protein (residues 1-72), with the main differences being the location of the N-loop (residues 10-22) relative to the C-terminal α-helix and the position of the side chain of phenylalanine 65 near the truncated dimerization interface (residues 67-72). NMR was used to analyze the interactions of monomeric IL-8 (1-66) with ND-CXCR1 (residues 1-38), a soluble polypeptide corresponding to the N-terminal portion of the ligand binding site (Binding Site-I) of the chemokine receptor CXCR1 in aqueous solution, and with 1TM-CXCR1 (residues 1-72), a membrane-associated polypeptide that includes the same N-terminal portion of the binding site, the first trans-membrane helix, and the first intracellular loop of the receptor in nanodiscs. The presence of neither the first transmembrane helix of the receptor nor the lipid bilayer significantly affected the interactions of IL-8 with Binding Site-I of CXCR1.

Indexed as

Binding SitesHumansInterleukin-8Lipid BilayersNuclear Magnetic Resonance, BiomolecularProtein BindingReceptors, Interleukin-8ACXCL8 protein, humanInterleukin-8Lipid BilayersReceptors, Interleukin-8AChemokineCXCL8GPCRIL-8NanodiscProtein structure

Identifiers

PMID29143165
PMCPMC5869024
OpenAlexW2768244904

What OpenQuestion holds

Textmetadata
LicenceTDM
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.