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PDBsum entry 2bo2

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protein ligands metals Protein-protein interface(s) links
Immune system PDB id
2bo2
Jmol
Contents
Protein chains
140 a.a. *
Ligands
CAC
Metals
_CA ×4
Waters ×32
* Residue conservation analysis
PDB id:
2bo2
Name: Immune system
Title: Egf domains 1,2,5 of human emr2, a 7-tm immune system molecule, in complex with calcium.
Structure: Egf-like module containing mucin-like hormone receptor-like 2 precursor. Chain: a, b. Fragment: egf domains 1,2 and 5,residues 25-118,212-260. Synonym: egf-like module emr2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: prep4.
Resolution:
2.60Å     R-factor:   0.239     R-free:   0.260
Authors: R.J.M.Abbott,I.Spendlove,P.Roversi,P.Teriete,V.Knott,P.A.Han J.M.Mcdonnell,S.M.Lea
Key ref: R.J.Abbott et al. (2007). Structural and functional characterization of a novel T cell receptor co-regulatory protein complex, CD97-CD55. J Biol Chem, 282, 22023-22032. PubMed id: 17449467
Date:
07-Apr-05     Release date:   09-Aug-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9UHX3  (EMR2_HUMAN) -  EGF-like module-containing mucin-like hormone receptor-like 2
Seq:
Struc:
 
Seq:
Struc:
823 a.a.
140 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biochemical function     G-protein coupled receptor activity     2 terms  

 

 
J Biol Chem 282:22023-22032 (2007)
PubMed id: 17449467  
 
 
Structural and functional characterization of a novel T cell receptor co-regulatory protein complex, CD97-CD55.
R.J.Abbott, I.Spendlove, P.Roversi, H.Fitzgibbon, V.Knott, P.Teriete, J.M.McDonnell, P.A.Handford, S.M.Lea.
 
  ABSTRACT  
 
CD97, the archetypal member of the EGF-TM7 protein family, is constitutively expressed on granulocytes and monocytes and rapidly up-regulated on T and B cells following activation. The key isoform of CD97 expressed on leukocytes binds the complement regulatory protein CD55 (also termed decay-accelerating factor). CD97 has been shown recently to mediate co-stimulation of T cells via CD55. Here, we demonstrate that blocking the interaction between CD55 on monocytes and CD97 on T cells leads to inhibition of proliferation and interferon-gamma secretion. This implies that bidirectional interactions between CD97 and CD55 are involved in T cell regulation. Structural studies presented here reveal the molecular basis for this activity. We have solved the structure of EMR2, a very close homolog of CD97, using x-ray crystallography. NMR-based chemical shift mapping of the EMR2-CD55 interaction has allowed us to generate a model for the CD97-CD55 complex. The structure of the complex reveals that the T cell and complement regulatory activities of CD55 occur on opposite faces of the molecule. This suggests that CD55 might simultaneously regulate both the innate and adaptive immune responses, and we have shown that CD55 can still regulate complement when bound to CD97.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19446531 S.A.Jensen, S.Iqbal, E.D.Lowe, C.Redfield, and P.A.Handford (2009).
Structure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins.
  Structure, 17, 759-768.
PDB code: 2w86
18660822 J.Cordle, S.Johnson, J.Z.Tay, P.Roversi, M.B.Wilkin, B.H.de Madrid, H.Shimizu, S.Jensen, P.Whiteman, B.Jin, C.Redfield, M.Baron, S.M.Lea, and P.A.Handford (2008).
A conserved face of the Jagged/Serrate DSL domain is involved in Notch trans-activation and cis-inhibition.
  Nat Struct Mol Biol, 15, 849-857.
PDB codes: 2vj2 2vj3
  17947652 P.N.Lalli, M.G.Strainic, F.Lin, M.E.Medof, and P.S.Heeger (2007).
Decay accelerating factor can control T cell differentiation into IFN-gamma-producing effector cells via regulating local C5a-induced IL-12 production.
  J Immunol, 179, 5793-5802.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.