PDBsum entry 1mi2

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protein Protein-protein interface(s) links
Cytokine PDB id
Protein chains
73 a.a. *
* Residue conservation analysis
PDB id:
Name: Cytokine
Title: Solution structure of murine macrophage inflammatory protein-2, nmr, 20 structures
Structure: Macrophage inflammatory protein-2. Chain: a, b. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
NMR struc: 20 models
Authors: W.Shao,L.F.Jerva,J.West,E.Lolis,B.I.Schweitzer
Key ref:
W.Shao et al. (1998). Solution structure of murine macrophage inflammatory protein-2. Biochemistry, 37, 8303-8313. PubMed id: 9622482 DOI: 10.1021/bi980112r
24-Oct-97     Release date:   29-Apr-98    
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Protein chains
Pfam   ArchSchema ?
P10889  (CXCL2_MOUSE) -  C-X-C motif chemokine 2
100 a.a.
73 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     neuron death   21 terms 
  Biochemical function     cytokine activity     3 terms  


DOI no: 10.1021/bi980112r Biochemistry 37:8303-8313 (1998)
PubMed id: 9622482  
Solution structure of murine macrophage inflammatory protein-2.
W.Shao, L.F.Jerva, J.West, E.Lolis, B.I.Schweitzer.
The solution structure of murine macrophage inflammatory protein-2 (MIP-2), a heparin-binding chemokine that is secreted in response to inflammatory stimuli, has been determined using two-dimensional homonuclear and heteronuclear NMR spectroscopy. Structure calculations were carried out by means of torsion-angle molecular dynamics using the program X-PLOR. The structure is based on a total of 2390 experimental restraints, comprising 2246 NOE-derived distance restraints, 44 distance restraints for 22 hydrogen bonds, and 100 torsion angle restraints. The structure is well-defined, with the backbone (N, Calpha, C) and heavy atom atomic rms distribution about the mean coordinates for residues 9-69 of the dimer being 0.57 +/- 0.16 A and 0.96 +/- 0.12 A, respectively. The N- and C-terminal residues (1-8 and 70-73, respectively) are disordered. The overall structure of the MIP-2 dimer is similar to that reported previously for the NMR structures of MGSA and IL-8 and consists of a six-stranded antiparallel beta-sheet (residue 25-29, 39-44, and 48-52) packed against two C-terminal antiparallel alpha-helices. A best fit superposition of the NMR structure of MIP-2 on the structures of MGSA, NAP-2, and the NMR and X-ray structures of IL-8 are 1.11, 1.02, 1.27, and 1.19 A, respectively, for the monomers, and 1.28, 1.10, 1.55, and 1.36 A, respectively, for the dimers (IL-8 residues 7-14 and 16-67, NAP-2 residues 25-84). At the tertiary level, the main differences between the MIP-2 solution structure and the IL-8, MGSA, and NAP-2 structures involve the N-terminal loop between residues 9-23 and the loops formed by residues 30-38 and residues 53-58. At the quaternary level, the difference between MIP-2 and IL-8, MGSA, or NAP-2 results from differing interhelical angles and separations.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20649939 J.Landsberg, E.Gaffal, M.Cron, J.Kohlmeyer, M.Renn, and T.Tüting (2010).
Autochthonous primary and metastatic melanomas in Hgf-Cdk4 R24C mice evade T-cell-mediated immune surveillance.
  Pigment Cell Melanoma Res, 23, 649-660.  
15979374 J.Y.Springael, E.Urizar, and M.Parmentier (2005).
Dimerization of chemokine receptors and its functional consequences.
  Cytokine Growth Factor Rev, 16, 611-623.  
14720307 T.Schountz, R.Green, B.Davenport, A.Buniger, T.Richens, J.J.Root, F.Davidson, C.H.Calisher, and B.J.Beaty (2004).
Cloning and characterization of deer mouse (Peromyscus maniculatus) cytokine and chemokine cDNAs.
  BMC Immunol, 5, 1.  
11889129 E.S.Kulo─člu, 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.  
12077146 K.Suetomi, D.Rojo, and J.Navarro (2002).
Identification of a signal transduction switch in the chemokine receptor CXCR1.
  J Biol Chem, 277, 31563-31566.  
11358512 W.Shao, E.Fernandez, A.Sachpatzidis, J.Wilken, D.A.Thompson, B.I.Schweitzer, and E.Lolis (2001).
CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure.
  Eur J Biochem, 268, 2948-2959.
PDB code: 1hhv
10727234 J.S.Laurence, C.Blanpain, J.W.Burgner, M.Parmentier, and P.J.LiWang (2000).
CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding.
  Biochemistry, 39, 3401-3409.  
11085746 T.Biedermann, M.Kneilling, R.Mailhammer, K.Maier, C.A.Sander, G.Kollias, S.L.Kunkel, L.Hültner, and M.Röcken (2000).
Mast cells control neutrophil recruitment during T cell-mediated delayed-type hypersensitivity reactions through tumor necrosis factor and macrophage inflammatory protein 2.
  J Exp Med, 192, 1441-1452.  
  10595530 A.C.Liwang, Z.X.Wang, Y.Sun, S.C.Peiper, and P.J.Liwang (1999).
The solution structure of the anti-HIV chemokine vMIP-II.
  Protein Sci, 8, 2270-2280.
PDB code: 1vmp
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