View source for 6fww


==GFP/KKK. A redesigned GFP with improved solubility==
<StructureSection load='6fww' size='340' side='right' caption='[[6fww]], [[Resolution|resolution]] 1.13&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fww]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FWW FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fww OCA], [http://pdbe.org/6fww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fww RCSB], [http://www.ebi.ac.uk/pdbsum/6fww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fww ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI]] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The aggregation propensity of each particular protein seems to be shaped by evolution according to its natural abundance in the cell. The production and downstream processing of recombinant polypeptides implies attaining concentrations that are orders of magnitude above their natural levels, often resulting in their aggregation; a phenomenon that precludes the marketing of many globular proteins for biomedical or biotechnological applications. Therefore, there is a huge interest in methods aimed to rise proteins solubility above their natural limits. Here, we demonstrate that an updated version of our AGGRESCAN 3D structural aggregation predictor, that now takes into account protein stability, allows designing mutations at specific positions in the structure that improve the solubility of proteins without compromising their conformation. Using this approach, we have designed a highly soluble variant of the Green Fluorescent Protein (GFP) and a human single-domain VH antibody displaying significantly reduced aggregation propensity. Overall, our data indicate that the solubility of unrelated proteins can be easily tuned by in silico-designed non-destabilizing amino acid changes at their surfaces.

Combining structural aggregation propensity and stability predictions to re-design protein solubility.,Gil-Garcia M, Bano-Polo M, Varejao N, Jamroz M, Kuriata A, Diaz Caballero M, Lascorz J, Morel B, Navarro S, Reverter D, Kmiecik S, Ventura S Mol Pharm. 2018 Jul 23. doi: 10.1021/acs.molpharmaceut.8b00341. PMID:30036481<ref>PMID:30036481</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fww" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aeqvi]]
[[Category: Diaz-Caballero, M]]
[[Category: Gil-Garcia, M]]
[[Category: Lascorz, J]]
[[Category: Navarro, S]]
[[Category: Reverter, D]]
[[Category: Varejao, N]]
[[Category: Ventura, S]]
[[Category: Aggregation prediction]]
[[Category: Aggrescan 3d]]
[[Category: Fluorescent protein]]
[[Category: Protein aggregation]]
[[Category: Protein design]]