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| [[Image:2q91.jpg|left|200px]]
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| <!-- | | ==Structure of the Ca2+-Bound Activated Form of the S100A4 Metastasis Factor== |
| The line below this paragraph, containing "STRUCTURE_2q91", creates the "Structure Box" on the page.
| | <StructureSection load='2q91' size='340' side='right'caption='[[2q91]], [[Resolution|resolution]] 1.63Å' scene=''> |
| You may change the PDB parameter (which sets the PDB file loaded into the applet) | | == Structural highlights == |
| or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| | <table><tr><td colspan='2'>[[2q91]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q91 FirstGlance]. <br> |
| or leave the SCENE parameter empty for the default display.
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.63Å</td></tr> |
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| | <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> |
| {{STRUCTURE_2q91| PDB=2q91 | SCENE= }}
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q91 OCA], [https://pdbe.org/2q91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q91 RCSB], [https://www.ebi.ac.uk/pdbsum/2q91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q91 ProSAT]</span></td></tr> |
| | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/S10A4_HUMAN S10A4_HUMAN] |
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q9/2q91_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </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=2q91 ConSurf]. |
| | <div style="clear:both"></div> |
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| '''Structure of the Ca2+-Bound Activated Form of the S100A4 Metastasis Factor'''
| | ==See Also== |
| | | *[[S100 proteins 3D structures|S100 proteins 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| S100A4, also known as mts1, is a member of the S100 family of Ca (2+)-binding proteins that is directly involved in tumor invasion and metastasis via interactions with specific protein targets, including nonmuscle myosin-IIA (MIIA). Human S100A4 binds two Ca (2+) ions with the typical EF-hand exhibiting an affinity that is nearly 1 order of magnitude tighter than that of the pseudo-EF-hand. To examine how Ca (2+) modifies the overall organization and structure of the protein, we determined the 1.7 A crystal structure of the human Ca (2+)-S100A4. Ca (2+) binding induces a large reorientation of helix 3 in the typical EF-hand. This reorganization exposes a hydrophobic cleft that is comprised of residues from the hinge region, helix 3, and helix 4, which afford specific target recognition and binding. The Ca (2+)-dependent conformational change is required for S100A4 to bind peptide sequences derived from the C-terminal portion of the MIIA rod with submicromolar affinity. In addition, the level of binding of Ca (2+) to both EF-hands increases by 1 order of magnitude in the presence of MIIA. NMR spectroscopy studies demonstrate that following titration with a MIIA peptide, the largest chemical shift perturbations and exchange broadening effects occur for residues in the hydrophobic pocket of Ca (2+)-S100A4. Most of these residues are not exposed in apo-S100A4 and explain the Ca (2+) dependence of formation of the S100A4-MIIA complex. These studies provide the foundation for understanding S100A4 target recognition and may support the development of reagents that interfere with S100A4 function.
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| ==About this Structure==
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| 2Q91 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q91 OCA].
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| ==Reference==
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| Structure of Ca(2+)-Bound S100A4 and Its Interaction with Peptides Derived from Nonmuscle Myosin-IIA., Malashkevich VN, Varney KM, Garrett SC, Wilder PT, Knight D, Charpentier TH, Ramagopal UA, Almo SC, Weber DJ, Bresnick AR, Biochemistry. 2008 May 6;47(18):5111-5126. Epub 2008 Apr 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18410126 18410126]
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| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| [[Category: Single protein]] | | [[Category: Large Structures]] |
| [[Category: Almo, S C.]] | | [[Category: Almo SC]] |
| [[Category: Bresnick, A R.]] | | [[Category: Bresnick AR]] |
| [[Category: Knight, D.]] | | [[Category: Knight D]] |
| [[Category: Malashkevich, V N.]] | | [[Category: Malashkevich VN]] |
| [[Category: Ramagopal, U A.]] | | [[Category: Ramagopal UA]] |
| [[Category: Calcium]]
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| [[Category: Ef-hand]]
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| [[Category: Metal binding protein]]
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| [[Category: Metastatic tumor]]
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| [[Category: Myosin]]
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| [[Category: S100a4]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 7 08:50:37 2008''
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