1mi2

<StructureSection load='1mi2' size='340' side='right'caption='[[1mi2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1mi2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MI2 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi2 OCA], [https://pdbe.org/1mi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mi2 RCSB], [https://www.ebi.ac.uk/pdbsum/1mi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mi2 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/CXCL2_MOUSE CXCL2_MOUSE]] Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst.

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== Publication Abstract from PubMed ==

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.

Solution structure of murine macrophage inflammatory protein-2.,Shao W, Jerva LF, West J, Lolis E, Schweitzer BI Biochemistry. 1998 Jun 9;37(23):8303-13. PMID:9622482<ref>PMID:9622482</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Lk3 transgenic mice]]

[[Category: Jerva, L F]]

[[Category: Lolis, E]]

[[Category: Schweitzer, B I]]

[[Category: Shao, W]]

[[Category: West, J]]

[[Category: Mip-2]]