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Cytokine PDB id
1eih
Jmol
Contents
Protein chain
73 a.a. *
* Residue conservation analysis
PDB id:
1eih
Name: Cytokine
Title: Solution structure of the human chemokine eotaxin-2
Structure: Eotaxin-2. Chain: a. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: K.L.Mayer,M.J.Stone
Key ref:
K.L.Mayer and M.J.Stone (2000). NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2. Biochemistry, 39, 8382-8395. PubMed id: 10913244 DOI: 10.1021/bi000523j
Date:
25-Feb-00     Release date:   06-Dec-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O00175  (CCL24_HUMAN) -  C-C motif chemokine 24
Seq:
Struc: 		119 a.a.
73 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     immune response   1 term 
  Biochemical function     chemokine activity     1 term  

 

 
DOI no: 10.1021/bi000523j Biochemistry 39:8382-8395 (2000)
PubMed id: 10913244  
 
 
NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2.
K.L.Mayer, M.J.Stone.
 
  ABSTRACT  
 
The human CC chemokine eotaxin-2 is a specific agonist for the chemokine receptor CCR3 and may play a role in the recruitment of eosinophils in allergic diseases and parasitic infections. We report the solution structure of eotaxin-2 determined using heteronuclear and triple resonance NMR methods. A family of 20 structures was calculated by hybrid distance geometry-simulated annealing from 854 NOE distance restraints, 48 dihedral angle restraints, and 12 hydrogen bond restraints. The structure of eotaxin-2 (73 amino acid residues) consists of a helical turn (residues 17-20) followed by a 3-stranded antiparallel beta-sheet (residues 22-26, 37-41, and 44-49) and an alpha-helix (residues 54-66). The N-loop (residues 9-16) is packed against both the sheet and the helix with the two conserved disulfide bonds tethering the N-terminal/N-loop region to the beta-sheet. The average backbone and heavy atom rmsd values of the 20 structures (residues 7-66) are 0.52 and 1.13 A, respectively. A linear peptide corresponding to the N-terminal region of CCR3 binds to eotaxin-2, inducing concentration-dependent chemical shift changes or line broadening of many residues. The distribution of these residues suggests that the peptide binds into an extended groove located at the interface between the N-loop and the beta2-beta3 hairpin. The receptor peptide may also interact with the N-terminus of the chemokine and part of the alpha-helix. Comparison of the eotaxin-2 structure with those of related chemokines indicates several structural features that may contribute to receptor specificity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21045060 S.Velankar, Y.Alhroub, A.Alili, C.Best, H.C.Boutselakis, S.Caboche, M.J.Conroy, J.M.Dana, G.van Ginkel, A.Golovin, S.P.Gore, A.Gutmanas, P.Haslam, M.Hirshberg, M.John, I.Lagerstedt, S.Mir, L.E.Newman, T.J.Oldfield, C.J.Penkett, J.Pineda-Castillo, L.Rinaldi, G.Sahni, G.Sawka, S.Sen, R.Slowley, A.W.Sousa da Silva, A.Suarez-Uruena, G.J.Swaminathan, M.F.Symmons, W.F.Vranken, M.Wainwright, and G.J.Kleywegt (2011).
PDBe: Protein Data Bank in Europe.
  Nucleic Acids Res, 39, D402-D410.  
20117133 J.L.Galzi, M.Hachet-Haas, D.Bonnet, F.Daubeuf, S.Lecat, M.Hibert, J.Haiech, and N.Frossard (2010).
Neutralizing endogenous chemokines with small molecules. Principles and potential therapeutic applications.
  Pharmacol Ther, 126, 39-55.  
19681642 A.Ravindran, P.R.Joseph, and K.Rajarathnam (2009).
Structural basis for differential binding of the interleukin-8 monomer and dimer to the CXCR1 N-domain: role of coupled interactions and dynamics.
  Biochemistry, 48, 8795-8805.  
19246006 L.S.Simpson, J.Z.Zhu, T.S.Widlanski, and M.J.Stone (2009).
Regulation of chemokine recognition by site-specific tyrosine sulfation of receptor peptides.
  Chem Biol, 16, 153-161.  
17222184 H.Fernando, G.T.Nagle, and K.Rajarathnam (2007).
Thermodynamic characterization of interleukin-8 monomer binding to CXCR1 receptor N-terminal domain.
  FEBS J, 274, 241-251.  
17644519 H.Jin, X.Shen, B.R.Baggett, X.Kong, and P.J.LiWang (2007).
The human CC chemokine MIP-1beta dimer is not competent to bind to the CCR5 receptor.
  J Biol Chem, 282, 27976-27983.  
17291188 S.J.Allen, S.E.Crown, and T.M.Handel (2007).
Chemokine: receptor structure, interactions, and antagonism.
  Annu Rev Immunol, 25, 787-820.  
17024562 L.Rajagopalan, and K.Rajarathnam (2006).
Structural basis of chemokine receptor function--a model for binding affinity and ligand selectivity.
  Biosci Rep, 26, 325-339.  
16963564 L.Zhang, M.Derider, M.A.McCornack, S.C.Jao, N.Isern, T.Ness, R.Moyer, and P.J.LiWang (2006).
Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta.
  Proc Natl Acad Sci U S A, 103, 13985-13990.
PDB codes: 2ffk 2fin
15039444 V.Petkovic, C.Moghini, S.Paoletti, M.Uguccioni, and B.Gerber (2004).
Eotaxin-3/CCL26 is a natural antagonist for CC chemokine receptors 1 and 5. A human chemokine with a regulatory role.
  J Biol Chem, 279, 23357-23363.  
12486712 K.L.Mayer, and M.J.Stone (2003).
Backbone dynamics of the CC-chemokine eotaxin-2 and comparison among the eotaxin group chemokines.
  Proteins, 50, 184-191.  
12411442 M.A.McCornack, C.K.Cassidy, and P.J.LiWang (2003).
The binding surface and affinity of monomeric and dimeric chemokine macrophage inflammatory protein 1 beta for various glycosaminoglycan disaccharides.
  J Biol Chem, 278, 1946-1956.  
11807180 E.J.Fernandez, and E.Lolis (2002).
Structure, function, and inhibition of chemokines.
  Annu Rev Pharmacol Toxicol, 42, 469-499.  
11889129 E.S.Kuloğlu, D.R.McCaslin, J.L.Markley, and B.F.Volkman (2002).
Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions.
  J Biol Chem, 277, 17863-17870.  
11980496 T.L.Nguyen, and E.Breslow (2002).
NMR analysis of the monomeric form of a mutant unliganded bovine neurophysin: comparison with the crystal structure of a neurophysin dimer.
  Biochemistry, 41, 5920-5930.
PDB codes: 1l5c 1l5d
11470923 B.T.Seet, R.Singh, C.Paavola, E.K.Lau, T.M.Handel, and G.McFadden (2001).
Molecular determinants for CC-chemokine recognition by a poxvirus CC-chemokine inhibitor.
  Proc Natl Acad Sci U S A, 98, 9008-9013.  
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 codes are shown on the right.