Evidence map›Paper›PMID 27411955›Full record

ArticleNature communications2016

Structural basis of transcobalamin recognition by human CD320 receptor.

Amer Alam, Jae-Sung Woo, Jennifer Schmitz, Bernadette Prinz, Katharina Root, Fan Chen, Joël S Bloch, Renato Zenobi, Kaspar P Locher

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 55 citations in OpenAlex.

  1. [Pathophysiology of hypervitaminosis B12: from origin to clinical event. Scoping review].Revista medica del Instituto Mexicano del Seguro Social · 2026
    Article
  2. Review
  3. Review
  4. CD320 Receptor and Vitamin B12 as Potential Targets for Anti-Cancer Therapy.International journal of molecular sciences · 2025
    Review
  5. Article
  6. Article
  7. Vitamin BInternational journal of molecular sciences · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. FTY720 requires vitamin BCell reports · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Bioprocess Strategies for Vitamin BBioengineering (Basel, Switzerland) · 2022
    Review
  17. Review
  18. Article
  19. Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

9 authors at 1 institution in 1 country.

Amer AlamDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
Jae-Sung WooDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.ORCID http://orcid.org/0000-0001-9163-3433
Jennifer SchmitzDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
Bernadette PrinzDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
Katharina RootDepartment of Chemistry and Applied Biosciences, ETH Zurich, 8093 Zurich, Switzerland.
Fan ChenDepartment of Chemistry and Applied Biosciences, ETH Zurich, 8093 Zurich, Switzerland.
Joël S BlochDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
Renato ZenobiDepartment of Chemistry and Applied Biosciences, ETH Zurich, 8093 Zurich, Switzerland.
Kaspar P LocherDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular uptake of vitamin B12 (cobalamin) requires capture of transcobalamin (TC) from the plasma by CD320, a ubiquitous cell surface receptor of the LDLR family. Here we present the crystal structure of human holo-TC in complex with the extracellular domain of CD320, visualizing the structural basis of the TC-CD320 interaction. The observed interaction chemistry can rationalize the high affinity of CD320 for TC and lack of haptocorrin binding. The in vitro affinity and complex stability of TC-CD320 were quantitated using a solid-phase binding assay and thermostability analysis. Stable complexes with TC were also observed for the disease-causing CD320ΔE88 mutant and for the isolated LDLR-A2 domain. We also determined the structure of the TC-CD320ΔE88 complex, which revealed only minor changes compared with the wild-type complex. Finally, we demonstrate significantly reduced in vitro affinity of TC for CD320 at low pH, recapitulating the proposed ligand release during the endocytic pathway.

Indexed as

Antigens, CDCrystallography, X-RayHistidineHumansHydrogen-Ion ConcentrationModels, MolecularProtein DomainsReceptors, Cell SurfaceStructure-Activity RelationshipTranscobalaminsAntigens, CDCD320 protein, humanHistidineReceptors, Cell SurfaceTranscobalamins

Identifiers

PMID27411955
PMCPMC4947154
OpenAlexW2469435513

What OpenQuestion holds

Textmetadata
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.