3fjd: Difference between revisions

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-{{Seed}}
-[[Image:3fjd.png|left|200px]]
-<!--
+==Crystal structure of L44F/F132W mutant of Human acidic fibroblast growth factor==
-The line below this paragraph, containing "STRUCTURE_3fjd", creates the "Structure Box" on the page.
+<StructureSection load='3fjd' size='340' side='right'caption='[[3fjd]], [[Resolution|resolution]] 1.90&Aring;' 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'>[[3fjd]] 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=3FJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FJD 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]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_3fjd|  PDB=3fjd  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fjd OCA], [https://pdbe.org/3fjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fjd RCSB], [https://www.ebi.ac.uk/pdbsum/3fjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fjd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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/fj/3fjd_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=3fjd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Protein biopharmaceuticals are an important and growing area of human therapeutics; however, the intrinsic property of proteins to adopt alternative conformations (such as during protein unfolding and aggregation) presents numerous challenges, limiting their effective application as biopharmaceuticals. Using fibroblast growth factor-1 as model system, we describe a cooperative interaction between the intrinsic property of thermostability and the reactivity of buried free-cysteine residues that can substantially modulate protein functional half-life. A mutational strategy that combines elimination of buried free cysteines and secondary mutations that enhance thermostability to achieve a substantial gain in functional half-life is described. Furthermore, the implementation of this design strategy utilizing stabilizing mutations within the core region resulted in a mutant protein that is essentially indistinguishable from wild type as regard protein surface and solvent structure, thus minimizing the immunogenic potential of the mutations. This design strategy should be generally applicable to soluble globular proteins containing buried free-cysteine residues.
-===Crystal structure of L44F/F132W mutant of Human acidic fibroblast growth factor===
+The interaction between thermodynamic stability and buried free cysteines in regulating the functional half-life of fibroblast growth factor-1.,Lee J, Blaber M J Mol Biol. 2009 Oct 16;393(1):113-27. Epub 2009 Aug 18. PMID:19695265<ref>PMID:19695265</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3fjd" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19695265}}, adds the Publication Abstract to the page
+*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19695265 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19695265}}
+__TOC__
+</StructureSection>
-==About this Structure==
-FJD is a 2 chains structure with sequences 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=3FJD OCA].
-==Reference==
-<ref group="xtra">PMID:19695265</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Blaber, M.]]
+[[Category: Large Structures]]
-[[Category: Lee, J.]]
+[[Category: Blaber M]]
-[[Category: Acetylation]]
+[[Category: Lee J]]
-[[Category: Angiogenesis]]
-[[Category: Beta-trefoil]]
-[[Category: Developmental protein]]
-[[Category: Differentiation]]
-[[Category: Growth factor]]
-[[Category: Heparin-binding]]
-[[Category: Hormone]]
-[[Category: Mitogen]]
-[[Category: Polymorphism]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 28 14:54:21 2010''