Journal:FEBS Journal:1

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One of the stable variants (IL-24B) was crystallized, its structure solved at 1.3 Å resolution and deposited to PDB under the code 6gg1. This structure together with the recently published crystal structure of the ternary complex of IL-24 fused to IL-22R1 and co-expressed with IL-20R2 (PDB ID [[6df3]]<ref name="Lub">PMID:30111632</ref>) allowed us to analyze the role of the mutated amino acid residues protein stability, flexibility, and binding to the cognate receptors (fig.2). Based on the analysis, we expressed a series of variants back engineered from the PROSS designed variant by changing the critical residues back to their wild types. We revealed that re-introduction of a single IL-24 wild type residue (T198) to the patch interacting with receptors 1 restored 80 % of the binding affinity and signaling capacity accompanied by an acceptable drop in the protein stability by 9°C.
One of the stable variants (IL-24B) was crystallized, its structure solved at 1.3 Å resolution and deposited to PDB under the code 6gg1. This structure together with the recently published crystal structure of the ternary complex of IL-24 fused to IL-22R1 and co-expressed with IL-20R2 (PDB ID [[6df3]]<ref name="Lub">PMID:30111632</ref>) allowed us to analyze the role of the mutated amino acid residues protein stability, flexibility, and binding to the cognate receptors (fig.2). Based on the analysis, we expressed a series of variants back engineered from the PROSS designed variant by changing the critical residues back to their wild types. We revealed that re-introduction of a single IL-24 wild type residue (T198) to the patch interacting with receptors 1 restored 80 % of the binding affinity and signaling capacity accompanied by an acceptable drop in the protein stability by 9°C.
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Additional references: <ref name="Goldenzweig">PMID:27425410</ref><ref name="Musil">PMID:28449074</ref><ref name="Frey">PMID:24636565</ref><ref name="Gorlich">PMID:24636567</ref>
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9. Goldenzweig A, Goldsmith M, Hill SE, Gertman O, Laurino P, Ashani Y, Dym O, Unger T, Albeck S, Prilusky J, Lieberman RL, Aharoni A, Silman I, Sussman JL, Tawfik DS & Fleishman SJ (2016) Automated Structure- and Sequence-Based Design of Proteins for High Bacterial Expression and Stability, Mol Cell 63, 337-346.
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10. Musil M, Stourac J, Bendl J, Brezovsky J, Prokop Z, Zendulka J, Martinek T, Bednar D & Damborsky J (2017) FireProt: web server for automated design of thermostable proteins, Nucleic Acids Res 45, W393-W399.
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11. Frey S & Gorlich D (2014) A new set of highly efficient, tag-cleaving proteases for purifying recombinant proteins, J Chrom A 1337, 95-105.
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12. Frey S & Gorlich D (2014) Purification of protein complexes of defined subunit stoichiometry using a set of orthogonal, tag-cleaving proteases, J Chrom A 1337, 106-15.
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<b>References</b><br>
<b>References</b><br>

Revision as of 12:26, 16 June 2019

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Alexander Berchansky, Jaime Prilusky

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