3fjb: Difference between revisions
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==Crystal structure of V31I mutant of Human acidic fibroblast growth factor== | ==Crystal structure of V31I mutant of Human acidic fibroblast growth factor== | ||
<StructureSection load='3fjb' size='340' side='right' caption='[[3fjb]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3fjb' size='340' side='right'caption='[[3fjb]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fjb]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3fjb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FJB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jqz|1jqz]], [[3fgm|3fgm]], [[3fj8|3fj8]], [[3fj9|3fj9]], [[3fja|3fja]], [[3fjc|3fjc]], [[3fjd|3fjd]], [[3fje|3fje]], [[3fjf|3fjf]], [[3fjh|3fjh]], [[3fji|3fji]], [[3fjj|3fjj]], [[3fjk|3fjk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jqz|1jqz]], [[3fgm|3fgm]], [[3fj8|3fj8]], [[3fj9|3fj9]], [[3fja|3fja]], [[3fjc|3fjc]], [[3fjd|3fjd]], [[3fje|3fje]], [[3fjf|3fjf]], [[3fjh|3fjh]], [[3fji|3fji]], [[3fjj|3fjj]], [[3fjk|3fjk]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FGF1, FGFA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FGF1, FGFA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fjb OCA], [https://pdbe.org/3fjb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fjb RCSB], [https://www.ebi.ac.uk/pdbsum/3fjb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fjb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Fibroblast growth factor|Fibroblast growth factor]] | *[[Fibroblast growth factor 3D structures|Fibroblast growth factor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Blaber, M]] | [[Category: Blaber, M]] | ||
[[Category: Lee, J]] | [[Category: Lee, J]] | ||
Revision as of 22:55, 20 October 2021
Crystal structure of V31I mutant of Human acidic fibroblast growth factorCrystal structure of V31I mutant of Human acidic fibroblast growth factor
Structural highlights
Function[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.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein 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. 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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