Evidence map›Paper›PMID 12773374›Full record

ArticleThe EMBO journal2003

Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76.

Maria Harkiolaki, Marc Lewitzky, Robert J C Gilbert, E Yvonne Jones, Roland P Bourette, Guy Mouchiroud, Holger Sondermann, Ismail Moarefi, Stephan M Feller

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

57 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Protein ubiquitination in T cell development.Frontiers in immunology · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Cooperative assembly of a four-molecule signaling complex formed upon T cell antigen receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Intracellular mechanisms of molecular recognition and sorting for transport of large extracellular matrix molecules.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Article
  20. Evolution of domain-peptide interactions to coadapt specificity and affinity to functional diversity.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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.

Maria HarkiolakiCancer Research UK Cell Signalling Group and Weatherall Institute of Molecular Medicine, Oxford, UK.
Marc Lewitzky
Robert J C Gilbert
E Yvonne Jones
Roland P Bourette
Guy Mouchiroud
Holger Sondermann
Ismail Moarefi
Stephan M Feller
Cancer Research UK · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

SH3 domains are protein recognition modules within many adaptors and enzymes. With more than 500 SH3 domains in the human genome, binding selectivity is a key issue in understanding the molecular basis of SH3 domain interactions. The Grb2-like adaptor protein Mona/Gads associates stably with the T-cell receptor signal transducer SLP-76. The crystal structure of a complex between the C-terminal SH3 domain (SH3C) of Mona/Gads and a SLP-76 peptide has now been solved to 1.7 A. The peptide lacks the canonical SH3 domain binding motif P-x-x-P and does not form a frequently observed poly-proline type II helix. Instead, it adopts a clamp-like shape around the circumfence of the SH3C beta-barrel. The central R-x-x-K motif of the peptide forms a 3(10) helix and inserts into a negatively charged double pocket on the SH3C while several other residues complement binding through hydrophobic interactions, creating a short linear SH3C binding epitope of uniquely high affinity. Interestingly, the SH3C displays ion-dependent dimerization in the crystal and in solution, suggesting a novel mechanism for the regulation of SH3 domain functions.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsCrystallography, X-RayDimerizationHumansHydrogen BondingIn Vitro TechniquesMiceModels, MolecularMolecular Sequence DataPhosphoproteinsPhylogenyAdaptor Proteins, Signal TransducingCarrier ProteinsGRAP2 protein, humanMona protein, mousePhosphoproteinsRecombinant ProteinsSLP-76 signal Transducing adaptor proteins

Identifiers

PMID12773374
PMCPMC156755
OpenAlexW2120096061

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.