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PDBsum entry 5fn8

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
5fn8

 

 

 

 

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Contents
Protein chains
178 a.a.
Ligands
NAG ×6
FLC
Waters ×56
PDB id:
5fn8
Name: Hydrolase
Title: Crystal structure of rat cd45 extracellular region, domains d3-d4
Structure: Receptor-type tyrosine-protein phosphatasE C. Chain: a, b. Fragment: extracellular region domains d3-d4, residues 357-546. Synonym: leukocyte common antigen, l-ca, t200, cd45. Engineered: yes
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: thymus. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: cho-k1.
Resolution:
2.45Å     R-factor:   0.216     R-free:   0.236
Authors: V.T.Chang,R.A.Fernandes,K.A.Ganzinger,S.F.Lee,C.Siebold,J.Mccoll, P.Jonsson,M.Palayret,K.Harlos,C.H.Coles,E.Y.Jones,Y.Lui,E.Huang, R.J.C.Gilbert,D.Klenerman,A.R.Aricescu,S.J.Davis
Key ref: V.T.Chang et al. (2016). Initiation of T cell signaling by CD45 segregation at 'close contacts'. Nat Immunol, 17, 574-582. PubMed id: 26998761 DOI: 10.1038/ni.3392
Date:
11-Nov-15     Release date:   23-Mar-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04157  (PTPRC_RAT) -  Receptor-type tyrosine-protein phosphatase C from Rattus norvegicus
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1273 a.a.
178 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.48  - protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate
O-phospho-L-tyrosyl-[protein]
+ H2O
= L-tyrosyl-[protein]
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
DOI no: 10.1038/ni.3392 Nat Immunol 17:574-582 (2016)
PubMed id: 26998761  
 
 
Initiation of T cell signaling by CD45 segregation at 'close contacts'.
V.T.Chang, R.A.Fernandes, K.A.Ganzinger, S.F.Lee, C.Siebold, J.McColl, P.Jönsson, M.Palayret, K.Harlos, C.H.Coles, E.Y.Jones, Y.Lui, E.Huang, R.J.Gilbert, D.Klenerman, A.R.Aricescu, S.J.Davis.
 
  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.
 

 

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