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5FN8

Crystal structure of rat CD45 extracellular region, domains d3-d4

Summary for 5FN8
Entry DOI10.2210/pdb5fn8/pdb
Related5FMV 5FN6 5FN7
DescriptorRECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE C, 2-acetamido-2-deoxy-beta-D-glucopyranose, CITRATE ANION, ... (4 entities in total)
Functional Keywordshydrolase, receptor protein tyrosine phosphatase c, cd45, ptprc
Biological sourceRATTUS NORVEGICUS (NORWAY RAT)
Total number of polymer chains2
Total formula weight44390.27
Authors
Primary citationChang, V.T.,Fernandes, R.A.,Ganzinger, K.A.,Lee, S.F.,Siebold, C.,Mccoll, J.,Jonsson, P.,Palayret, M.,Harlos, K.,Coles, C.H.,Jones, E.Y.,Lui, Y.,Huang, E.,Gilbert, R.J.,Klenerman, D.,Aricescu, A.R.,Davis, S.J.
Initiation of T Cell Signaling by Cd45 Segregation at 'Close Contacts'.
Nat.Immunol., 17:574-, 2016
Cited by
PubMed Abstract: It has been proposed that the local segregation of kinases and the tyrosine phosphatase CD45 underpins T cell antigen receptor (TCR) triggering, but how such segregation occurs and whether it can initiate signaling is unclear. Using structural and biophysical analysis, we show that the extracellular region of CD45 is rigid and extends beyond the distance spanned by TCR-ligand complexes, implying that sites of TCR-ligand engagement would sterically exclude CD45. We also show that the formation of 'close contacts', new structures characterized by spontaneous CD45 and kinase segregation at the submicron-scale, initiates signaling even when TCR ligands are absent. Our work reveals the structural basis for, and the potent signaling effects of, local CD45 and kinase segregation. TCR ligands have the potential to heighten signaling simply by holding receptors in close contacts.
PubMed: 26998761
DOI: 10.1038/NI.3392
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

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數據於2024-11-06公開中

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