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PDBsum entry 1esr

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Cytokine PDB id
1esr

 

 

 

 

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Contents
Protein chain
76 a.a. *
Waters ×89
* Residue conservation analysis
PDB id:
1esr
Name: Cytokine
Title: Crystal structure of human monocyte chemotactic protein-2
Structure: Monocyte chemotactic protein 2. Chain: a. Synonym: mcp-2. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
Resolution:
2.00Å     R-factor:   0.244     R-free:   0.320
Authors: J.Blaszczyk,X.Ji
Key ref:
J.Blaszczyk et al. (2000). Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors. Biochemistry, 39, 14075-14081. PubMed id: 11087354 DOI: 10.1021/bi0009340
Date:
10-Apr-00     Release date:   06-Dec-00    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P80075  (CCL8_HUMAN) -  C-C motif chemokine 8 from Homo sapiens
Seq:
Struc:
99 a.a.
76 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1021/bi0009340 Biochemistry 39:14075-14081 (2000)
PubMed id: 11087354  
 
 
Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors.
J.Blaszczyk, E.V.Coillie, P.Proost, J.V.Damme, G.Opdenakker, G.D.Bujacz, J.M.Wang, X.Ji.
 
  ABSTRACT  
 
Monocyte chemotactic protein 2 (MCP-2) is a CC chemokine that utilizes multiple cellular receptors to attract and activate human leukocytes. MCP-2 is a potent inhibitor of HIV-1 by virtue of its high-affinity binding to the receptor CCR5, one of the major coreceptors for HIV-1. Although a few structures of CC chemokines have been reported, none of these was determined with the N-terminal pyroglutamic acid residue (pGlu1) and a complete C-terminus. pGlu1 is essential for the chemotactic activity of MCP-2. Recombinant MCP-2 has Gln1 at the N terminus, 12-15% of which cyclizes automatically and forms pGlu1. The chemotactic activity of such MCP-2 mixture, which contains 12-15% pGlu1-form and 85-88% Gln1-form protein, is approximately 10 times lower when compared with that of fully cyclized MCP-2 preparation. Therefore, this chemokine is practically inactive without pGlu1. We have determined the complete crystal structure of MCP-2 that contains both pGlu1 and an intact C-terminus. With the existence of pGlu1, the conformation of the N-terminus allows two additional interactions between the two subunits of MCP-2 dimer: a hydrogen bond between pGlu1 and Asn17 and a salt bridge between Asp3 and Arg18. Consequently, both pGlu1 are anchored and buried, and thereby, both N-terminal regions are protected against protease degradation. We have also observed not previously reported extended helical nature of the C terminal region, which covers residues 58-74.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20077567 J.W.Murphy, H.Yuan, Y.Kong, Y.Xiong, and E.J.Lolis (2010).
Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family.
  Proteins, 78, 1331-1337.
PDB codes: 3gv3 3hp3
19034645 S.Cochran, C.P.Li, and V.Ferro (2009).
A surface plasmon resonance-based solution affinity assay for heparan sulfate-binding proteins.
  Glycoconj J, 26, 577-587.  
18323622 C.Barinka, A.Prahl, and J.Lubkowski (2008).
Structure of human monocyte chemoattractant protein 4 (MCP-4/CCL13).
  Acta Crystallogr D Biol Crystallogr, 64, 273-278.
PDB code: 2ra4
17960578 J.B.De Jesus, P.Cuervo, M.Junqueira, C.Britto, F.C.Silva-Filho, L.Sabóia-Vahia, L.J.González, and G.Barbosa Domont (2007).
Application of two-dimensional electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for proteomic analysis of the sexually transmitted parasite Trichomonas vaginalis.
  J Mass Spectrom, 42, 1463-1473.  
17291188 S.J.Allen, S.E.Crown, and T.M.Handel (2007).
Chemokine: receptor structure, interactions, and antagonism.
  Annu Rev Immunol, 25, 787-820.  
16820060 J.S.Gillis (2006).
Microarray evidence of glutaminyl cyclase gene expression in melanoma: implications for tumor antigen specific immunotherapy.
  J Transl Med, 4, 27.  
16840324 P.L.Arnold, and D.H.Fremont (2006).
Structural determinants of chemokine binding by an Ectromelia virus-encoded decoy receptor.
  J Virol, 80, 7439-7449.
PDB code: 2grk
16803905 S.E.Crown, Y.Yu, M.D.Sweeney, J.A.Leary, and T.M.Handel (2006).
Heterodimerization of CCR2 chemokines and regulation by glycosaminoglycan binding.
  J Biol Chem, 281, 25438-25446.  
16033763 Y.Yu, M.D.Sweeney, O.M.Saad, S.E.Crown, A.R.Hsu, T.M.Handel, and J.A.Leary (2005).
Chemokine-glycosaminoglycan binding: specificity for CCR2 ligand binding to highly sulfated oligosaccharides using FTICR mass spectrometry.
  J Biol Chem, 280, 32200-32208.  
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.  
11807180 E.J.Fernandez, and E.Lolis (2002).
Structure, function, and inhibition of chemokines.
  Annu Rev Pharmacol Toxicol, 42, 469-499.  
11830659 H.Lortat-Jacob, A.Grosdidier, and A.Imberty (2002).
Structural diversity of heparan sulfate binding domains in chemokines.
  Proc Natl Acad Sci U S A, 99, 1229-1234.  
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.

 

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