Evidence map›Paper›PMID 19168783›Full record

ArticleBlood2009

The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties.

Paul R Stabach, Ivana Simonović, Miranda A Ranieri, Michael S Aboodi, Thomas A Steitz, Miljan Simonović, Jon S Morrow

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Reticulocyte Maturation.Membranes · 2022
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. α2 and α3 helices of dystrophin R16 and R17 frame a microdomain in the α1 helix of dystrophin R17 for neuronal NOS binding.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Paul R StabachDepartment of Pathology, Yale University, New Haven, CT 06520, USA.
Ivana Simonović
Miranda A Ranieri
Michael S Aboodi
Thomas A Steitz
Miljan Simonović
Jon S Morrow
Yale University · US

Funding

MEMBRANE SKELETAL CONTROL IN HEMOLYTIC DISORDERSR01HL028560 · NHLBI · YALE UNIVERSITY · PI MORROW, JON S · 1985 to 2011
$3.3M
Topographic Spectrin Assembly in the Renal Tubule CellR01DK043812 · NIDDK · YALE UNIVERSITY · PI MORROW, JON S · 1991 to 2007
$1.9M
Howard Hughes Medical InstituteNHLBI NIH HHS R01 HL028560NHLBI NIH HHS R01-HL28560NIDDK NIH HHS R01 DK043812NIDDK NIH HHS R01-DK43812
6 · The paper itself

Abstract

Spectrin and ankyrin participate in membrane organization, stability, signal transduction, and protein targeting; their interaction is critical for erythrocyte stability. Repeats 14 and 15 of betaI-spectrin are crucial for ankyrin recognition, yet the way spectrin binds ankyrin while preserving its repeat structure is unknown. We have solved the crystal structure of the betaI-spectrin 14,15 di-repeat unit to 2.1 A resolution and found 14 residues critical for ankyrin binding that map to the end of the helix C of repeat 14, the linker region, and the B-C loop of repeat 15. The tilt (64 degrees) across the 14,15 linker is greater than in any published di-repeat structure, suggesting that the relative positioning of the two repeats is important for ankyrin binding. We propose that a lack of structural constraints on linker and inter-helix loops allows proteins containing spectrin-like di-repeats to evolve diverse but specific ligand-recognition sites without compromising the structure of the repeat unit. The linker regions between repeats are thus critical determinants of both spectrin's flexibility and polyfunctionality. The putative coupling of flexibility and ligand binding suggests a mechanism by which spectrin might participate in mechanosensory regulation.

Indexed as

AlanineAmino Acid MotifsAmino Acid SequenceAnkyrinsBinding SitesCrystallography, X-RayHumansLigandsMechanotransduction, CellularModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingProtein FoldingProtein Interaction MappingProtein Structure, TertiaryAlanineAnkyrinsLigandsSpectrin

Identifiers

PMID19168783
PMCPMC2689040
OpenAlexW2007486980

What OpenQuestion holds

Textmetadata
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.