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3cqa

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{{Seed}}
 
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[[Image:3cqa.png|left|200px]]
 
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<!--
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==Crystal structure of human fibroblast growth factor-1 with mutations Glu81Ala and Lys101Ala==
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The line below this paragraph, containing "STRUCTURE_3cqa", creates the "Structure Box" on the page.
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<StructureSection load='3cqa' size='340' side='right'caption='[[3cqa]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3cqa]] 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=3CQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CQA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#8491;</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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_3cqa| PDB=3cqa | SCENE= }}
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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=3cqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cqa OCA], [https://pdbe.org/3cqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cqa RCSB], [https://www.ebi.ac.uk/pdbsum/3cqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cqa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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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/cq/3cqa_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3cqa 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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Large-volume protein crystals are a prerequisite for neutron diffraction studies and their production represents a bottleneck in obtaining neutron structures. Many protein crystals that permit the collection of high-resolution X-ray diffraction data are inappropriate for neutron diffraction owing to a plate-type morphology that limits the crystal volume. Human fibroblast growth factor 1 crystallizes in a plate morphology that yields atomic resolution X-ray diffraction data but has insufficient volume for neutron diffraction. The thin physical dimension has been identified as corresponding to the b cell edge and the X-ray structure identified a solvent-mediated crystal contact adjacent to position Glu81 that was hypothesized to limit efficient crystal growth in this dimension. In this report, a series of mutations at this crystal contact designed to both reduce side-chain entropy and replace the solvent-mediated interface with direct side-chain contacts are reported. The results suggest that improved crystal growth is achieved upon the introduction of direct crystal contacts, while little improvement is observed with side-chain entropy-reducing mutations alone.
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===Crystal structure of human fibroblast growth factor-1 with mutations Glu81Ala and Lys101Ala===
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Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.,Meher AK, Blaber SI, Lee J, Honjo E, Kuroki R, Blaber M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt, 11):1136-40. Epub 2009 Oct 30. PMID:19923735<ref>PMID:19923735</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3cqa" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19923735}}, adds the Publication Abstract to the page
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*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19923735 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19923735}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3CQA is a 2 chains structure of 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=3CQA OCA].
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==Reference==
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<ref group="xtra">PMID:19923735</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Blaber, M.]]
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[[Category: Large Structures]]
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[[Category: Honjo, E.]]
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[[Category: Blaber M]]
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[[Category: Kuroki, R.]]
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[[Category: Honjo E]]
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[[Category: Lee, J.]]
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[[Category: Kuroki R]]
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[[Category: Meher, A K.]]
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[[Category: Lee J]]
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[[Category: Somasundaram, T.]]
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[[Category: Meher AK]]
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[[Category: Acetylation]]
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[[Category: Somasundaram T]]
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[[Category: Angiogenesis]]
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[[Category: Crystal packing]]
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[[Category: Developmental protein]]
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[[Category: Differentiation]]
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[[Category: Growth factor]]
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[[Category: Heparin-binding]]
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[[Category: Hormone]]
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[[Category: Mitogen]]
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[[Category: Polymorphism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 6 09:00:18 2010''
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Current revision

Crystal structure of human fibroblast growth factor-1 with mutations Glu81Ala and Lys101Ala

PDB ID 3cqa

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