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2ki6
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2ki6.jpg|left|200px]] | ||
| - | < | + | ==The FGF1-S100A13-C2A hetero-hexameric complex structure: A component in the non-classical pathway for FGF1 secretion== |
| - | + | <StructureSection load='2ki6' size='340' side='right'caption='[[2ki6]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2ki6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KI6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DLY:D-LYSINE'>DLY</scene></td></tr> | |
| - | -- | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYT1, SVP65, SYT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), FGF1, FGFA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), S100A13 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2ki6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ki6 OCA], [https://pdbe.org/2ki6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ki6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ki6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ki6 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/S10AD_HUMAN S10AD_HUMAN]] Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity).<ref>PMID:12746488</ref> <ref>PMID:20863990</ref> [[https://www.uniprot.org/uniprot/SYT1_HUMAN SYT1_HUMAN]] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. [[https://www.uniprot.org/uniprot/FGF1_HUMAN FGF1_HUMAN]] Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro.<ref>PMID:8663044</ref> <ref>PMID:16597617</ref> <ref>PMID:20145243</ref> | ||
| + | == 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/ki/2ki6_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=2ki6 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fibroblast growth factors (FGFs) are key regulators of cell proliferation, tumor-induced angiogenesis, and migration. FGFs are essential for early embryonic development, organ formation, and angiogenesis. FGF1 also plays an important role in inflammation, wound healing, and restenosis. The biological effects of FGF1 are mediated through the activation of the four transmembrane phosphotyrosine kinase fibroblast growth factor receptors in the presence of heparin sulfate proteoglycans and, therefore, require the release of the protein into the extracellular space. FGF1 is exported through a non-classical release pathway involving the formation of a specific multiprotein complex. The protein constituents of this complex include FGF1, S100A13, and the p40 form of synaptotagmin 1 (Syt1). Because FGF1 plays an important role in tumor formation, it is clear that preventing the formation of the multiprotein complex would be an effective strategy to inhibit a wide range of cancers. To understand the molecular events in the FGF1 release pathway, we studied the FGF1-S100A13 tetrameric and FGF1-S100A13-C2A hexameric complex structures, which are both complexes possibly formed during the non-classical pathway of FGF1 release. | ||
| - | + | The heterohexameric complex structure, a component in the non-classical pathway for fibroblast growth factor 1 (FGF1) secretion.,Mohan SK, Rani SG, Yu C J Biol Chem. 2010 May 14;285(20):15464-75. Epub 2010 Mar 10. PMID:20220137<ref>PMID:20220137</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2ki6" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]] | |
| - | [[Category: | + | *[[S100 proteins 3D structures|S100 proteins 3D structures]] |
| - | [[Category: Krishna, S M | + | *[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]] |
| - | [[Category: Rani, S G | + | == References == |
| - | [[Category: Yu, C | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Krishna, S M]] | ||
| + | [[Category: Rani, S G]] | ||
| + | [[Category: Yu, C]] | ||
[[Category: Acetylation]] | [[Category: Acetylation]] | ||
[[Category: Alternative splicing]] | [[Category: Alternative splicing]] | ||
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[[Category: Synapse]] | [[Category: Synapse]] | ||
[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 10 14:17:01 2010'' | ||
Current revision
The FGF1-S100A13-C2A hetero-hexameric complex structure: A component in the non-classical pathway for FGF1 secretion
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Categories: Human | Large Structures | Krishna, S M | Rani, S G | Yu, C | Acetylation | Alternative splicing | Angiogenesis | C2a | Calcium | Cell junction | Cytoplasmic vesicle | Developmental protein | Differentiation | Fgf1 | Fgf1-s100a13-c2a hetero-hexameric complex | Glycoprotein | Growth factor | Heparin-binding | Lipoprotein | Membrane | Metal-binding | Mitogen | Palmitate | Phosphoprotein | Polymorphism | Protein transport | S100a13 | Synapse | Transmembrane
