1qql: Difference between revisions

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<StructureSection load='1qql' size='340' side='right'caption='[[1qql]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1qql' size='340' side='right'caption='[[1qql]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qql]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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>
<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>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qqk|1qqk]]</div></td></tr>
</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>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FGF7_RAT FGF7_RAT]] Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation.  
[https://www.uniprot.org/uniprot/FGF7_RAT FGF7_RAT] Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qql" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Luo, Y]]
[[Category: Rattus norvegicus]]
[[Category: McKeehan, W L]]
[[Category: Luo Y]]
[[Category: Pelletier, H]]
[[Category: McKeehan WL]]
[[Category: Ye, S]]
[[Category: Pelletier H]]
[[Category: Beta-trefoil]]
[[Category: Ye S]]
[[Category: Hormone-growth factor complex]]
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