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| - | [[Image:1wy9.gif|left|200px]] | |
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| - | {{Structure
| + | ==Crystal structure of microglia-specific protein, Iba1== |
| - | |PDB= 1wy9 |SIZE=350|CAPTION= <scene name='initialview01'>1wy9</scene>, resolution 2.10Å
| + | <StructureSection load='1wy9' size='340' side='right'caption='[[1wy9]], [[Resolution|resolution]] 2.10Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
| + | <table><tr><td colspan='2'>[[1wy9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WY9 FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | |GENE= Aif1, Iba1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wy9 OCA], [https://pdbe.org/1wy9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wy9 RCSB], [https://www.ebi.ac.uk/pdbsum/1wy9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wy9 ProSAT]</span></td></tr> |
| - | |RELATEDENTRY= | + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wy9 OCA], [http://www.ebi.ac.uk/pdbsum/1wy9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wy9 RCSB]</span>
| + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/AIF1_MOUSE AIF1_MOUSE] Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation.<ref>PMID:11722645</ref> <ref>PMID:10934045</ref> <ref>PMID:11500035</ref> <ref>PMID:11916959</ref> <ref>PMID:14756805</ref> |
| - | | + | == Evolutionary Conservation == |
| - | '''Crystal structure of microglia-specific protein, Iba1'''
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | | + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | ==Overview== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wy/1wy9_consurf.spt"</scriptWhenChecked> |
| - | The ionized calcium-binding adaptor molecule 1 (Iba1) with 147 amino acid residues has been identified as a calcium-binding protein, expressed specifically in microglia/macrophages, and is expected to be a key factor in membrane ruffling, which is a typical feature of activated microglia. We have determined the crystal structure of human Iba1 in a Ca(2+)-free form and mouse Iba1 in a Ca(2+)-bound form, to a resolution of 1.9 A and 2.1 A, respectively. X-ray structures of Iba1 revealed a compact, single-domain protein with two EF-hand motifs, showing similarity in overall topology to partial structures of the classical EF-hand proteins troponin C and calmodulin. In mouse Iba1, the second EF-hand contains a bound Ca(2+), but the first EF-hand does not, which is often the case in S100 proteins, suggesting that Iba1 has S100 protein-like EF-hands. The molecular conformational change induced by Ca(2+)-binding of Iba1 is different from that found in the classical EF-hand proteins and/or S100 proteins, which demonstrates that Iba1 has an unique molecular switching mechanism dependent on Ca(2+)-binding, to interact with target molecules.
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==About this Structure== | + | </jmolCheckbox> |
| - | 1WY9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WY9 OCA].
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wy9 ConSurf]. |
| - | | + | <div style="clear:both"></div> |
| - | ==Reference== | + | == References == |
| - | X-ray structures of the microglia/macrophage-specific protein Iba1 from human and mouse demonstrate novel molecular conformation change induced by calcium binding., Yamada M, Ohsawa K, Imai Y, Kohsaka S, Kamitori S, J Mol Biol. 2006 Dec 1;364(3):449-57. Epub 2006 Sep 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17011575 17011575]
| + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Single protein]]
| + | [[Category: Imai Y]] |
| - | [[Category: Imai, Y.]] | + | [[Category: Kamitori S]] |
| - | [[Category: Kamitori, S.]] | + | [[Category: Kohsaka S]] |
| - | [[Category: Kohsaka, S.]] | + | [[Category: Yamada M]] |
| - | [[Category: Yamada, M.]] | + | |
| - | [[Category: calucium binding]]
| + | |
| - | [[Category: ef-hand]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:42:35 2008''
| + | |
| Structural highlights
Function
AIF1_MOUSE Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Watano K, Iwabuchi K, Fujii S, Ishimori N, Mitsuhashi S, Ato M, Kitabatake A, Onoe K. Allograft inflammatory factor-1 augments production of interleukin-6, -10 and -12 by a mouse macrophage line. Immunology. 2001 Nov;104(3):307-16. PMID:11722645
- ↑ Ohsawa K, Imai Y, Kanazawa H, Sasaki Y, Kohsaka S. Involvement of Iba1 in membrane ruffling and phagocytosis of macrophages/microglia. J Cell Sci. 2000 Sep;113 ( Pt 17):3073-84. PMID:10934045
- ↑ Sasaki Y, Ohsawa K, Kanazawa H, Kohsaka S, Imai Y. Iba1 is an actin-cross-linking protein in macrophages/microglia. Biochem Biophys Res Commun. 2001 Aug 17;286(2):292-7. PMID:11500035 doi:http://dx.doi.org/10.1006/bbrc.2001.5388
- ↑ Kanazawa H, Ohsawa K, Sasaki Y, Kohsaka S, Imai Y. Macrophage/microglia-specific protein Iba1 enhances membrane ruffling and Rac activation via phospholipase C-gamma -dependent pathway. J Biol Chem. 2002 May 31;277(22):20026-32. Epub 2002 Mar 26. PMID:11916959 doi:http://dx.doi.org/10.1074/jbc.M109218200
- ↑ Ohsawa K, Imai Y, Sasaki Y, Kohsaka S. Microglia/macrophage-specific protein Iba1 binds to fimbrin and enhances its actin-bundling activity. J Neurochem. 2004 Feb;88(4):844-56. PMID:14756805
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