Evidence map›Paper›PMID 12554651›Full record

ArticleThe EMBO journal2003

Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.

Keisuke Hamada, Toshiyuki Shimizu, Shigenobu Yonemura, Shoichiro Tsukita, Sachiko Tsukita, Toshio Hakoshima

Abstract read
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 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

72 citing papers in PubMed.

  1. SARS-CoV-2 S assembly into virions facilitated by host ERM proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  4. A bipartite NLS motif mediates the nuclear import ofFrontiers in cell and developmental biology · 2024
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  6. Review
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  9. Spectrum ofGenes · 2021
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  13. Review
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  15. Article
  16. Molecular physiology and pathophysiology of stromal interaction molecules.Experimental biology and medicine (Maywood, N.J.) · 2018
    Review
  17. Structural basis of kindlin-mediated integrin recognition and activation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Review
  20. Myosin MyTH4-FERM structures highlight important principles of convergent evolution.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article

12 more citing papers are in PubMed but not listed here.

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

6 authors.

Keisuke HamadaStructural Biology Laboratory, Nara Institute of Science and Technology and CREST, Japan Science and Technology Corporation, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan.
Toshiyuki Shimizu
Shigenobu Yonemura
Shoichiro Tsukita
Sachiko Tsukita
Toshio Hakoshima

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ERM (ezrin/radixin/moesin) proteins recognize the cytoplasmic domains of adhesion molecules in the formation of the membrane-associated cytoskeleton. Here we report the crystal structure of the radixin FERM (4.1 and ERM) domain complexed with the ICAM-2 cytoplasmic peptide. The non-polar region of the ICAM-2 peptide contains the RxxTYxVxxA sequence motif to form a beta-strand followed by a short 3(10)-helix. It binds the groove of the phosphotyrosine-binding (PTB)-like subdomain C mediated by a beta-beta association and several side-chain interactions. The binding mode of the ICAM-2 peptide to the FERM domain is distinct from that of the NPxY motif-containing peptide binding to the canonical PTB domain. Mutation analyses based on the crystal structure reveal the determinant elements of recognition and provide the first insights into the physical link between adhesion molecules and ERM proteins.

Indexed as

Protein Structure, SecondaryProtein Structure, TertiaryAmino Acid SequenceAnimalsAntigens, CDbeta CateninBlood ProteinsCell Adhesion MoleculesCell MembraneCrystallography, X-RayCytoskeletal ProteinsCytoskeletonHumansMacromolecular SubstancesMembrane ProteinsMiceAntigens, CDbeta CateninBlood ProteinsCell Adhesion MoleculesCTNNB1 protein, humanCTNNB1 protein, mouseCytoskeletal ProteinsICAM2 protein, humanMacromolecular SubstancesMembrane ProteinsPeptidesradixinTrans-Activators

Identifiers

PMID12554651
PMCPMC140724

What OpenQuestion holds

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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.