ArticleThe Journal of experimental medicine2005
Structural basis for the function and regulation of the receptor protein tyrosine phosphatase CD45.
Article in The Journal of experimental medicine, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 55 papers.
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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.
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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.
Who cites it
55 citing papers in PubMed, 106 citations in OpenAlex.
- Clustering of the T-cell receptor complex may facilitate T-cell activation by stretching of CD3ζ cytoplasmic tails.European biophysics journal : EBJ · 2026Article
- CD45 as a multifunctional target in immune regulation and therapeutic delivery.Journal of translational medicine · 2026Review
- Adenoviral E3/49K: CD45-targeted immune evasion and therapeutic potential.Frontiers in cellular and infection microbiology · 2026Review
- Towards a unifying model for B-cell receptor triggering.Nature reviews. Immunology · 2025Review
- Predicting protein interactions of the kinase Lck critical to T cell modulation.Structure (London, England : 1993) · 2024Article
- Development of Novel Phosphonodifluoromethyl-Containing Phosphotyrosine Mimetics and a First-In-Class, Potent, Selective, and Bioavailable Inhibitor of Human CDC14 Phosphatases.Journal of medicinal chemistry · 2024Article
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- Defining the Cell Surface Cysteinome using Two-step Enrichment Proteomics.bioRxiv : the preprint server for biology · 2023Article
- Clustering of phosphatase RPTPα promotes Src signaling and the arthritogenic action of synovial fibroblasts.Science signaling · 2023Article
- Enforced Dimerization of CD45 by the Adenovirus E3/49K Protein Inhibits T Cell Receptor Signaling.Journal of virology · 2023Article
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- Structural insights into the pSer/pThr dependent regulation of the SHP2 tyrosine phosphatase in insulin and CD28 signaling.Nature communications · 2022Article
- Substrate-selective positive allosteric modulation of PTPRD's phosphatase by flavonols.Biochemical pharmacology · 2022Article
- Protein Tyrosine Phosphatases: A new paradigm in an old signaling system?Advances in cancer research · 2021Review
- RPTPα phosphatase activity is allosterically regulated by the membrane-distal catalytic domain.The Journal of biological chemistry · 2020Article
- A head-to-toe dimerization has physiological relevance for ligand-induced inactivation of protein tyrosine receptor type Z.The Journal of biological chemistry · 2019Article
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- Fullerene derivatives act as inhibitors of leukocyte common antigen based on molecular dynamics simulations.RSC advances · 2018Article
- Targeting Receptor-Type Protein Tyrosine Phosphatases with Biotherapeutics: Is Outside-in Better than Inside-Out?Molecules (Basel, Switzerland) · 2018Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
CD45 is the prototypic member of transmembrane receptor-like protein tyrosine phosphatases (RPTPs) and has essential roles in immune functions. The cytoplasmic region of CD45, like many other RPTPs, contains two homologous protein tyrosine phosphatase domains, active domain 1 (D1) and catalytically impaired domain 2 (D2). Here, we report crystal structure of the cytoplasmic D1D2 segment of human CD45 in native and phosphotyrosyl peptide-bound forms. The tertiary structures of D1 and D2 are very similar, but doubly phosphorylated CD3zeta immunoreceptor tyrosine-based activation motif peptide binds only the D1 active site. The D2 "active site" deviates from the other active sites significantly to the extent that excludes any possibility of catalytic activity. The relative orientation of D1 and D2 is very similar to that observed in leukocyte common antigen-related protein with both active sites in an open conformation and is restrained through an extensive network of hydrophobic interactions, hydrogen bonds, and salt bridges. This crystal structure is incompatible with the wedge model previously suggested for CD45 regulation.
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What OpenQuestion holds
Registered trials
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.