Evidence map›Paper›PMID 30417120›Full record

ArticleCommunications biology2018

An asparagine/glycine switch governs product specificity of human N-terminal methyltransferase NTMT2.

Cheng Dong, Guangping Dong, Li Li, Licheng Zhu, Wolfram Tempel, Yanli Liu, Rong Huang, Jinrong Min

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Structural basis of tRNA recognition by the mNature structural & molecular biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Chemical Biology of Protein N-Terminal Methyltransferases.Chembiochem : a European journal of chemical biology · 2019
    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

8 authors at 3 institutions in 3 countries.

Cheng DongStructural Genomics Consortium, University of Toronto, Toronto, M5G1L7, ON, Canada.ORCID http://orcid.org/0000-0002-2891-8759
Guangping DongDepartment of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN, 47907, USA.
Li LiStructural Genomics Consortium, University of Toronto, Toronto, M5G1L7, ON, Canada.
Licheng ZhuStructural Genomics Consortium, University of Toronto, Toronto, M5G1L7, ON, Canada.
Wolfram TempelStructural Genomics Consortium, University of Toronto, Toronto, M5G1L7, ON, Canada.
Yanli LiuStructural Genomics Consortium, University of Toronto, Toronto, M5G1L7, ON, Canada.
Rong HuangDepartment of Medicinal Chemistry and Molecular Pharmacology, Center for Cancer Research, Institute for Drug Discovery, Purdue University, West Lafayette, IN, 47907, USA. huang-r@purdue.edu.
Jinrong MinStructural Genomics Consortium, University of Toronto, Toronto, M5G1L7, ON, Canada. jr.min@utoronto.ca.
University of Toronto · CAPurdue University West Lafayette · USJinggangshan University · CN

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
Protein N-terminal Methylation Mechanisms and InhibitionR01GM117275 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI HUANG, RONG · 2016 to 2025
$3.2M
Discovery of small molecule inhibitors for protein N-terminal methyltransferaseU01CA214649 · NCI · PURDUE UNIVERSITY · PI HUANG, RONG · 2017 to 2019
$1.1M
NCI NIH HHS P30 CA023168NCI NIH HHS U01 CA214649NIGMS NIH HHS R01 GM117275Wellcome Trust
6 · The paper itself

Abstract

α-N-terminal methylation of proteins is an important post-translational modification that is catalyzed by two different N-terminal methyltransferases, namely NTMT1 and NTMT2. Previous studies have suggested that NTMT1 is a tri-methyltransferase, whereas NTMT2 is a mono-methyltransferase. Here, we report the first crystal structures, to our knowledge, of NTMT2 in binary complex with S-adenosyl-L-methionine as well as in ternary complex with S-adenosyl-L-homocysteine and a substrate peptide. Our structural observations combined with biochemical studies reveal that NTMT2 is also able to di-/tri-methylate the GPKRIA peptide and di-methylate the PPKRIA peptide, otherwise it is predominantly a mono-methyltransferase. The residue N89 of NTMT2 serves as a gatekeeper residue that regulates the binding of unmethylated versus monomethylated substrate peptide. Structural comparison of NTMT1 and NTMT2 prompts us to design a N89G mutant of NTMT2 that can profoundly alter its catalytic activities and product specificities.

Identifiers

PMID30417120
PMCPMC6214909
OpenAlexW2898688174

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.