Evidence map›Paper›PMID 28757145›Full record

ArticleStructure (London, England : 1993)2017

Structural Basis for Substrate Recognition by the Ankyrin Repeat Domain of Human DHHC17 Palmitoyltransferase.

Raffaello Verardi, Jin-Sik Kim, Rodolfo Ghirlando, Anirban Banerjee

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Biochemistry · 2026
    Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Ankyrin-B is lipid-modified byFrontiers in physiology · 2023
    Article
  19. Review
  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

4 authors.

Raffaello VerardiUnit on Structural and Chemical Biology of Membrane Proteins, Cell Biology and Neurobiology Branch, National Institute of Child Health and Human Development, National Institutes of Health, 35A Convent Drive, Bethesda, MD 20892, USA.
Jin-Sik KimUnit on Structural and Chemical Biology of Membrane Proteins, Cell Biology and Neurobiology Branch, National Institute of Child Health and Human Development, National Institutes of Health, 35A Convent Drive, Bethesda, MD 20892, USA.
Rodolfo GhirlandoLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Anirban BanerjeeUnit on Structural and Chemical Biology of Membrane Proteins, Cell Biology and Neurobiology Branch, National Institute of Child Health and Human Development, National Institutes of Health, 35A Convent Drive, Bethesda, MD 20892, USA. Electronic address: anirban.banerjee@nih.gov.

Funding

Structural and chemical biology of membrane proteinsZIAHD008928 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BANERJEE, ANIRBAN · 2013 to 2025
$34.5M
Intramural NIH HHS ZIA HD008928
6 · The paper itself

Abstract

DHHC enzymes catalyze palmitoylation, a major post-translational modification that regulates a number of key cellular processes. There are up to 24 DHHCs in mammals and hundreds of substrate proteins that get palmitoylated. However, how DHHC enzymes engage with their substrates is still poorly understood. There is currently no structural information about the interaction between any DHHC enzyme and protein substrates. In this study we have investigated the structural and thermodynamic bases of interaction between the ankyrin repeat domain of human DHHC17 (ANK17) and Snap25b. We solved a high-resolution crystal structure of the complex between ANK17 and a peptide fragment of Snap25b. Through structure-guided mutagenesis, we discovered key residues in DHHC17 that are critically important for interaction with Snap25b. We further extended our finding by showing that the same residues are also crucial for the interaction of DHHC17 with Huntingtin, one of its most physiologically relevant substrates.

Indexed as

AcyltransferasesAdaptor Proteins, Signal TransducingAmino Acid MotifsAnkyrin RepeatBinding SitesCrystallography, X-RayHEK293 CellsHumansHuntingtin ProteinModels, MolecularMutationNerve Tissue ProteinsPalmitatesProtein DomainsSubstrate SpecificitySynaptosomal-Associated Protein 25AcyltransferasesAdaptor Proteins, Signal TransducingHTT protein, humanHuntingtin ProteinNerve Tissue ProteinsPalmitatesSnap25 protein, mouseSynaptosomal-Associated Protein 25ZDHHC17 protein, humanDHHCDHHC17Huntingtinpalmitoylationpalmitoyltransferaseposttranslational modificationprotein lipidationprotein-protein interactionSnap25bX-ray crystallography

Identifiers

PMID28757145
PMCPMC5599134

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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.