PMID- 9712872
OWN - NLM
STAT- MEDLINE
DCOM- 19980924
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 273
IP  - 35
DP  - 1998 Aug 28
TI  - Solution structure of eotaxin, a chemokine that selectively recruits eosinophils 
      in allergic inflammation.
PG  - 22471-9
AB  - The solution structure of the CCR3-specific chemokine, eotaxin, has been 
      determined by NMR spectroscopy. The quaternary structure of eotaxin was 
      investigated by ultracentrifugation and NMR, and it was found to be in 
      equilibrium between monomer and dimer under a wide range of conditions. At pH </= 
      5 and low ionic strength, eotaxin was found to be predominantly a monomer. The 
      three-dimensional structure of the eotaxin monomer solved at pH 5.0 revealed that 
      it has a typical chemokine fold, which includes a 3-stranded beta-sheet and an 
      overlying alpha-helix. Except for the N-terminal residues (residues 1-8), the 
      core of the protein is well defined. The eotaxin structure is compared with the 
      chemokines regulated upon activation, normal T-cell expressed and secreted 
      (RANTES) and monocyte chemoattractant protein-1 (MCP-1); eotaxin binds only CC 
      chemokine receptor CCR3, whereas RANTES binds many receptors including CCR3, and 
      MCP-1 binds a distinct receptor, CCR2. The RMSD of the eotaxin ensemble of 
      structures with the RANTES average minimized monomeric subunit is 5.52 +/- 0.87 A 
      over all backbone atoms and 1.14 +/- 0.09 A over backbone atoms of residues 11-28 
      and 34-65. The most important difference between the structures is in the 
      N-terminal residues that are unstructured in eotaxin but structured in RANTES and 
      MCP-1. Several residues in the loop region of RANTES show similar packing in 
      eotaxin (residues 11-17). As the N-terminal and loop regions have been shown to 
      be critical for receptor binding and signaling, this structure will be useful for 
      determining the basis for CCR3 selectivity of the eotaxin.
FAU - Crump, M P
AU  - Crump MP
AD  - Protein Engineering Network of Centres of Excellence (PENCE) and Department of 
      Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2S2.
FAU - Rajarathnam, K
AU  - Rajarathnam K
FAU - Kim, K S
AU  - Kim KS
FAU - Clark-Lewis, I
AU  - Clark-Lewis I
FAU - Sykes, B D
AU  - Sykes BD
LA  - eng
SI  - PDB/1EOT
SI  - PDB/2EOT
SI  - PDB/4155
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Chemokine CCL11)
RN  - 0 (Chemokines)
RN  - 0 (Chemokines, CC)
RN  - 0 (Cytokines)
RN  - 0 (Solutions)
SB  - IM
MH  - Amino Acid Sequence
MH  - Asthma/*pathology
MH  - Chemokine CCL11
MH  - Chemokines/chemistry
MH  - *Chemokines, CC
MH  - Cytokines/*chemistry/physiology
MH  - Dimerization
MH  - Eosinophils/*pathology
MH  - Hydrogen-Ion Concentration
MH  - Magnetic Resonance Spectroscopy
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Structure, Tertiary
MH  - Sequence Homology, Amino Acid
MH  - Solutions
EDAT- 1998/08/26 00:00
MHDA- 1998/08/26 00:01
CRDT- 1998/08/26 00:00
PHST- 1998/08/26 00:00 [pubmed]
PHST- 1998/08/26 00:01 [medline]
PHST- 1998/08/26 00:00 [entrez]
AID - S0021-9258(18)48749-2 [pii]
AID - 10.1074/jbc.273.35.22471 [doi]
PST - ppublish
SO  - J Biol Chem. 1998 Aug 28;273(35):22471-9. doi: 10.1074/jbc.273.35.22471.