5FN8: Crystal Structure Of Rat Cd45 Extracellular Region, Domains D3-d4

Citation:
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.
PDB ID: 5FN8Download
MMDB ID: 137736
PDB Deposition Date: 2015/11/11
Updated in MMDB: 2016/05
Experimental Method:
x-ray diffraction
Resolution: 2.45  Å
Source Organism:
Similar Structures:
Biological Unit for 5FN8: monomeric; determined by author
Molecular Components in 5FN8
Label Count Molecule
Protein (1 molecule)
1
Receptor-type Tyrosine-protein Phosphatase C(Gene symbol: Ptprc)
Molecule annotation
Chemicals (5 molecules)
1
4
2
1
* Click molecule labels to explore molecular sequence information.

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