1qql

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(New page: 200px<br /> <applet load="1qql" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qql, resolution 2.3&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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[[Image:1qql.gif|left|200px]]<br />
 
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<applet load="1qql" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qql, resolution 2.3&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 7/1 CHIMERA'''<br />
 
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==Overview==
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==THE CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 7/1 CHIMERA==
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Stromal cell-derived FGF-7 binds and activates only the resident FGFR2IIIb, in epithelial cells while FGF-1 and FGF-2 exhibit a broader interaction, with multiple isoforms of FGFR. Here we report the structure of FGF-7 that, has been solved to 3.1 A resolution by molecular replacement with the, structure of a dual function chimera of FGF-7 and FGF-1 (FGF-7/1) which, was resolved to 2.3 A. Comparison of the FGF-7 structure to that of FGF-1, and FGF-2 revealed the strongly conserved Calpha backbone among the three, FGF polypeptides and the surface hydrophobic patch that forms the primary, receptor-binding domain. In contrast, a decrease and dispersion of the, positive surface charge density characterized the heparin-binding domain, of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with, heparin. A simple heparin hexasaccharide that cocrystallized with FGF-1, and FGF-2 and protected both against protease in solution failed to, exhibit the same properties with FGF-7. In contrast to FGF-1 and FGF-2, protection of FGF-7 was enhanced by heparin oligosaccharides of increased, length with those exhibiting a 3-O-sulfate being the most effective., Protection of FGF-7 required interaction with specifically the fraction of, crude heparin retained on antithrombin affinity columns. Conversely, heparin enriched by affinity for immobilized FGF-7 exhibited anti-factor, Xa activity similar to that purified on an antithrombin affinity matrix., In contrast, an FGF-1 affinity matrix enriched the fraction of crude, heparin with low anti-factor Xa activity. The results provide a structural, basis to suggest that the unique FGF-7 heparin-binding (HB) domain, underlies a specific restriction in respect to composition and length of, the heparan sulfate motif that may impact specificity of localization, stability, and trafficking of FGF-7 in the microenvironment, and formation, and activation of the FGFR2IIIb kinase signaling complex in epithelial, cells.
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<StructureSection load='1qql' size='340' side='right'caption='[[1qql]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qql]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QQL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qql OCA], [https://pdbe.org/1qql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qql RCSB], [https://www.ebi.ac.uk/pdbsum/1qql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qql ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FGF7_RAT FGF7_RAT] Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qq/1qql_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1qql ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Stromal cell-derived FGF-7 binds and activates only the resident FGFR2IIIb in epithelial cells while FGF-1 and FGF-2 exhibit a broader interaction with multiple isoforms of FGFR. Here we report the structure of FGF-7 that has been solved to 3.1 A resolution by molecular replacement with the structure of a dual function chimera of FGF-7 and FGF-1 (FGF-7/1) which was resolved to 2.3 A. Comparison of the FGF-7 structure to that of FGF-1 and FGF-2 revealed the strongly conserved Calpha backbone among the three FGF polypeptides and the surface hydrophobic patch that forms the primary receptor-binding domain. In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin. A simple heparin hexasaccharide that cocrystallized with FGF-1 and FGF-2 and protected both against protease in solution failed to exhibit the same properties with FGF-7. In contrast to FGF-1 and FGF-2, protection of FGF-7 was enhanced by heparin oligosaccharides of increased length with those exhibiting a 3-O-sulfate being the most effective. Protection of FGF-7 required interaction with specifically the fraction of crude heparin retained on antithrombin affinity columns. Conversely, heparin enriched by affinity for immobilized FGF-7 exhibited anti-factor Xa activity similar to that purified on an antithrombin affinity matrix. In contrast, an FGF-1 affinity matrix enriched the fraction of crude heparin with low anti-factor Xa activity. The results provide a structural basis to suggest that the unique FGF-7 heparin-binding (HB) domain underlies a specific restriction in respect to composition and length of the heparan sulfate motif that may impact specificity of localization, stability, and trafficking of FGF-7 in the microenvironment, and formation and activation of the FGFR2IIIb kinase signaling complex in epithelial cells.
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==Disease==
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Structural basis for interaction of FGF-1, FGF-2, and FGF-7 with different heparan sulfate motifs.,Ye S, Luo Y, Lu W, Jones RB, Linhardt RJ, Capila I, Toida T, Kan M, Pelletier H, McKeehan WL Biochemistry. 2001 Dec 4;40(48):14429-39. PMID:11724555<ref>PMID:11724555</ref>
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Known diseases associated with this structure: Aplasia of lacrimal and salivary glands OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602115 602115]], LADD syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602115 602115]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1QQL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus_+_homo_sapiens Rattus norvegicus + homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QQL OCA].
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</div>
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<div class="pdbe-citations 1qql" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structural basis for interaction of FGF-1, FGF-2, and FGF-7 with different heparan sulfate motifs., Ye S, Luo Y, Lu W, Jones RB, Linhardt RJ, Capila I, Toida T, Kan M, Pelletier H, McKeehan WL, Biochemistry. 2001 Dec 4;40(48):14429-39. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11724555 11724555]
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*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
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[[Category: Rattus norvegicus + homo sapiens]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Luo, Y.]]
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__TOC__
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[[Category: McKeehan, W.L.]]
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</StructureSection>
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[[Category: Pelletier, H.]]
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[[Category: Homo sapiens]]
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[[Category: Ye, S.]]
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[[Category: Large Structures]]
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[[Category: beta-trefoil]]
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[[Category: Rattus norvegicus]]
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[[Category: Luo Y]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:55:36 2007''
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[[Category: McKeehan WL]]
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[[Category: Pelletier H]]
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[[Category: Ye S]]

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THE CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 7/1 CHIMERA

PDB ID 1qql

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