8u5a: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
Line 8: Line 8:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8u5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8u5a OCA], [https://pdbe.org/8u5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8u5a RCSB], [https://www.ebi.ac.uk/pdbsum/8u5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8u5a ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8u5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8u5a OCA], [https://pdbe.org/8u5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8u5a RCSB], [https://www.ebi.ac.uk/pdbsum/8u5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8u5a ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Natural proteins are highly optimized for function but are often difficult to produce at a scale suitable for biotechnological applications due to poor expression in heterologous systems, limited solubility, and sensitivity to temperature. Thus, a general method that improves the physical properties of native proteins while maintaining function could have wide utility for protein-based technologies. Here, we show that the deep neural network ProteinMPNN, together with evolutionary and structural information, provides a route to increasing protein expression, stability, and function. For both myoglobin and tobacco etch virus (TEV) protease, we generated designs with improved expression, elevated melting temperatures, and improved function. For TEV protease, we identified multiple designs with improved catalytic activity as compared to the parent sequence and previously reported TEV variants. Our approach should be broadly useful for improving the expression, stability, and function of biotechnologically important proteins.
Improving Protein Expression, Stability, and Function with ProteinMPNN.,Sumida KH, Nunez-Franco R, Kalvet I, Pellock SJ, Wicky BIM, Milles LF, Dauparas J, Wang J, Kipnis Y, Jameson N, Kang A, De La Cruz J, Sankaran B, Bera AK, Jimenez-Oses G, Baker D J Am Chem Soc. 2024 Jan 9. doi: 10.1021/jacs.3c10941. PMID:38194293<ref>PMID:38194293</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8u5a" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 15:35, 13 August 2026

Improving protein expression, stability, and function with ProteinMPNN

8u5a, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA