1p63

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(New page: 200px<br /> <applet load="1p63" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p63, resolution 1.60&Aring;" /> '''Human Acidic Fibrob...)
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[[Image:1p63.gif|left|200px]]<br />
 
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<applet load="1p63" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p63, resolution 1.60&Aring;" />
 
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'''Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I)'''<br />
 
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==Overview==
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==Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I)==
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An alternative core packing group, involving a set of five positions, has, been introduced into human acidic FGF-1. This alternative group was, designed so as to constrain the primary structure within the core region, to the same threefold symmetry present in the tertiary structure of the, protein fold (the beta-trefoil superfold). The alternative core is, essentially indistinguishable from the WT core with regard to structure, stability, and folding kinetics. The results show that the beta-trefoil, superfold is compatible with a threefold symmetric constraint on the core, region, as might be the case if the superfold arose as a result of gene, duplication/fusion events. Furthermore, this new core arrangement can form, the basis of a structural "building block" that can greatly simplify the, de novo design of beta-trefoil proteins by using symmetric structural, complementarity. Remaining asymmetry within the core appears to be related, to asymmetry in the tertiary structure associated with receptor and, heparin binding functionality of the growth factor.
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<StructureSection load='1p63' size='340' side='right'caption='[[1p63]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1p63]] 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=1P63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P63 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]] 1.6&#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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p63 OCA], [https://pdbe.org/1p63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p63 RCSB], [https://www.ebi.ac.uk/pdbsum/1p63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p63 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/p6/1p63_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=1p63 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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An alternative core packing group, involving a set of five positions, has been introduced into human acidic FGF-1. This alternative group was designed so as to constrain the primary structure within the core region to the same threefold symmetry present in the tertiary structure of the protein fold (the beta-trefoil superfold). The alternative core is essentially indistinguishable from the WT core with regard to structure, stability, and folding kinetics. The results show that the beta-trefoil superfold is compatible with a threefold symmetric constraint on the core region, as might be the case if the superfold arose as a result of gene duplication/fusion events. Furthermore, this new core arrangement can form the basis of a structural "building block" that can greatly simplify the de novo design of beta-trefoil proteins by using symmetric structural complementarity. Remaining asymmetry within the core appears to be related to asymmetry in the tertiary structure associated with receptor and heparin binding functionality of the growth factor.
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==Disease==
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Accommodation of a highly symmetric core within a symmetric protein superfold.,Brych SR, Kim J, Logan TM, Blaber M Protein Sci. 2003 Dec;12(12):2704-18. PMID:14627732<ref>PMID:14627732</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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1P63 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P63 OCA].
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</div>
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<div class="pdbe-citations 1p63" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Accommodation of a highly symmetric core within a symmetric protein superfold., Brych SR, Kim J, Logan TM, Blaber M, Protein Sci. 2003 Dec;12(12):2704-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14627732 14627732]
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*[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Blaber, M.]]
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[[Category: Blaber M]]
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[[Category: Brych, S.R.]]
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[[Category: Brych SR]]
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[[Category: Kim, J.]]
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[[Category: Kim J]]
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[[Category: Logan, T.M.]]
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[[Category: Logan TM]]
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[[Category: FMT]]
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[[Category: SO4]]
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[[Category: beta-trefoil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:40:36 2007''
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Current revision

Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I)

PDB ID 1p63

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