5FMV

Crystal structure of human CD45 extracellular region, domains d1-d4

Summary for 5FMV

• Entry DOI: 10.2210/pdb5fmv/pdb
• Related: 5FN6 5FN7 5FN8
• Descriptor: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE C, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION (3 entities in total)
• Functional Keywords: hydrolase, receptor protein tyrosine phosphatase, cd45, ptprc
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 86214.94

Authors

Chang, 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.C.,Klenerman, D.,Aricescu, A.R.,Davis, S.J. (deposition date: 2015-11-09, release date: 2016-03-23, Last modification date: 2024-10-16)

Primary citation

Chang, 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

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

Experimental method

X-RAY DIFFRACTION (2.9 Å)