Evidence map›Paper›PMID 16772286›Full record

ArticleThe Journal of biological chemistry2006

Crystal structure of the second LNS/LG domain from neurexin 1alpha: Ca2+ binding and the effects of alternative splicing.

Lauren R Sheckler, Lisa Henry, Shuzo Sugita, Thomas C Südhof, Gabby Rudenko

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Predicting RNA Structure Utilizing Attention from Pretrained Language Models.Journal of chemical information and modeling · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Laminin G-like domains: dystroglycan-specific lectins.Current opinion in structural biology · 2019
    Review
  11. Neurexins - versatile molecular platforms in the synaptic cleft.Current opinion in structural biology · 2019
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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.

Lauren R ShecklerLife Sciences Institute and Department of Pharmacology, The University of Michigan, Ann Arbor, Michigan 48109-2216, USA.
Lisa Henry
Shuzo Sugita
Thomas C Südhof
Gabby Rudenko

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI CINGOLANI, GINO · 1985 to 2011
$23.8M
Synaptic Organizers: Dynamic Regulation of Trans-synaptic BridgesR01MH077303 · NIMH · UNIVERSITY OF TEXAS MED BR GALVESTON · PI Gabrielle Rudenko · 2006 to 2026
$8.2M
NCRR NIH HHS P41 RR001646NIGMS NIH HHS DMR-0225180NIMH NIH HHS R01 MH077303NIMH NIH HHS R01MH077303
6 · The paper itself

Abstract

Neurexins mediate protein interactions at the synapse, playing an essential role in synaptic function. Extracellular domains of neurexins, and their fragments, bind a distinct profile of different proteins regulated by alternative splicing and Ca2+. The crystal structure of n1alpha_LNS#2 (the second LNS/LG domain of bovine neurexin 1alpha) reveals large structural differences compared with n1alpha_LNS#6 (or n1beta_LNS), the only other LNS/LG domain for which a structure has been determined. The differences overlap the so-called hyper-variable surface, the putative protein interaction surface that is reshaped as a result of alternative splicing. A Ca2+-binding site is revealed at the center of the hyper-variable surface next to splice insertion sites. Isothermal titration calorimetry indicates that the Ca2+-binding site in n1alpha_LNS#2 has low affinity (Kd approximately 400 microm). Ca2+ binding ceases to be measurable when an 8- or 15-residue splice insert is present at the splice site SS#2 indicating that alternative splicing can affect Ca2+-binding sites of neurexin LNS/LG domains. Our studies initiate a framework for the putative protein interaction sites of neurexin LNS/LG domains. This framework is essential to understand how incorporation of alternative splice inserts expands the information from a limited set of neurexin genes to produce a large array of synaptic adhesion molecules with potentially very different synaptic function.

Indexed as

Alternative SplicingAnimalsCalciumCattleCrystallography, X-RayEscherichia coliGlycoproteinsKineticsModels, MolecularMolecular ConformationNeuropeptidesProtein BindingProtein Structure, TertiaryCalciumGlycoproteinsneurexophilinNeuropeptides

Identifiers

PMID16772286
PMCPMC2293330

What OpenQuestion holds

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Registered trials

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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.