Evidence map›Paper›PMID 26900151›Full record

ArticleThe Journal of biological chemistry2016

Ligand Binding Induces Conformational Changes in Human Cellular Retinol-binding Protein 1 (CRBP1) Revealed by Atomic Resolution Crystal Structures.

Josie A Silvaroli, Jason M Arne, Sylwia Chelstowska, Philip D Kiser, Surajit Banerjee, Marcin Golczak

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Advances and therapeutic opportunities in visual cycle modulation.Progress in retinal and eye research · 2025
    Review
  4. Retinoic acid signaling and metabolism in heart failure.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Retinol-binding protein 2 (RBP2): More than just dietary retinoid uptake.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2022
    Review
  12. Retinal pigment epithelium 65 kDa protein (RPE65): An update.Progress in retinal and eye research · 2022
    Review
  13. Aldehyde Oxidase Contributes to All-Drug metabolism and disposition: the biological fate of chemicals · 2021
    Article
  14. The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  15. Retinol-binding protein 2 (RBP2): biology and pathobiology.Critical reviews in biochemistry and molecular biology · 2020
    Review
  16. Article
  17. Article
  18. Structural biology of 11-The Biochemical journal · 2018
    Review
  19. Article
  20. Article
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 3 institutions in 2 countries.

Josie A SilvaroliFrom the Department of Pharmacology and.
Jason M ArneFrom the Department of Pharmacology and.
Sylwia ChelstowskaFrom the Department of Pharmacology and the Laboratory of Hematology and Flow Cytometry, Department of Hematology, Military Institute of Medicine, Warsaw 04-141, Poland.
Philip D KiserFrom the Department of Pharmacology and the Research Service, Louis Stokes Cleveland Veterans Affairs Medical Center, Cleveland, Ohio 44106.
Surajit Banerjeethe Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14850, and the Northeastern Collaborative Access Team, Argonne National Laboratory, Argonne, Illinois 60439.
Marcin GolczakFrom the Department of Pharmacology and the Cleveland Center for Membrane and Structural Biology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106, mxg149@case.edu.
Case Western Reserve University · USCornell University · USWojskowy Instytut Medycyny Lotniczej · PL

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Regulation of vitamin A metabolism in the eyeR01EY023948 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI GOLCZAK, MARCIN BERNARD · 2014 to 2023
$3.8M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Studies on visual cycles and their relevance to age-related macular degenerationIK2BX002683 · VA · VETERANS HEALTH ADMINISTRATION · PI KISER, PHILIP DAVID · 2015 to 2019
–
BLRD VA IK2 BX002683NCRR NIH HHS S10 RR029205NEI NIH HHS R01 EY023948NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

Important in regulating the uptake, storage, and metabolism of retinoids, cellular retinol-binding protein 1 (CRBP1) is essential for trafficking vitamin A through the cytoplasm. However, the molecular details of ligand uptake and targeted release by CRBP1 remain unclear. Here we report the first structure of CRBP1 in a ligand-free form as well as ultra-high resolution structures of this protein bound to either all-trans-retinol or retinylamine, the latter a therapeutic retinoid that prevents light-induced retinal degeneration. Superpositioning of human apo- and holo-CRBP1 revealed major differences within segments surrounding the entrance to the retinoid-binding site. These included α-helix II and hairpin turns between β-strands βC-βD and βE-βF as well as several side chains, such as Phe-57, Tyr-60, and Ile-77, that change their orientations to accommodate the ligand. Additionally, we mapped hydrogen bond networks inside the retinoid-binding cavity and demonstrated their significance for the ligand affinity. Analyses of the crystallographic B-factors indicated several regions with higher backbone mobility in the apoprotein that became more rigid upon retinoid binding. This conformational flexibility of human apo-CRBP1 facilitates interaction with the ligands, whereas the more rigid holoprotein structure protects the labile retinoid moiety during vitamin A transport. These findings suggest a mechanism of induced fit upon ligand binding by mammalian cellular retinol-binding proteins.

Indexed as

Crystallography, X-RayHumansHydrogen BondingLigandsProtein Structure, SecondaryRetinol-Binding Proteins, CellularVitamin ALigandsRBP1 protein, humanRetinol-Binding Proteins, CellularVitamin Alipid transportretinal metabolismretinoid-binding proteinretinolvitamin A

Identifiers

PMID26900151
PMCPMC4861425
OpenAlexW2282949853

What OpenQuestion holds

Textmetadata
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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.