5l2h

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Current revision (12:42, 6 March 2024) (edit) (undo)
 
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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=5l2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l2h OCA], [https://pdbe.org/5l2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l2h RCSB], [https://www.ebi.ac.uk/pdbsum/5l2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l2h 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=5l2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l2h OCA], [https://pdbe.org/5l2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l2h RCSB], [https://www.ebi.ac.uk/pdbsum/5l2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l2h ProSAT]</span></td></tr>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Targeted delivery of therapeutic payloads to specific tissues and cell types is an important component of modern pharmaceutical development. Antibodies or other scaffold proteins can provide the cellular address for delivering a covalently linked therapeutic via specific binding to cell-surface receptors. Optimization of the conjugation site on the targeting protein, linker chemistry and intracellular trafficking pathways can all influence the efficiency of delivery and potency of the drug candidate. In this study, we describe a comprehensive engineering experiment for an EGFR binding Centyrin, a highly stable fibronectin type III (FN3) domain, wherein all possible single-cysteine replacements were evaluated for expression, purification, conjugation efficiency, retention of target binding, biophysical properties and delivery of a cytotoxic small molecule payload. Overall, 26 of the 94 positions were identified as ideal for cysteine modification, conjugation and drug delivery. Conjugation-tolerant positions were mapped onto a crystal structure of the Centyrin, providing a structural context for interpretation of the mutagenesis experiment and providing a foundation for a Centyrin-targeted delivery platform.
 
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Engineering a targeted delivery platform using Centyrins.,Goldberg SD, Cardoso RM, Lin T, Spinka-Doms T, Klein D, Jacobs SA, Dudkin V, Gilliland G, O'Neil KT Protein Eng Des Sel. 2016 Oct 13. PMID:27737926<ref>PMID:27737926</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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<div class="pdbe-citations 5l2h" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
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Current revision

Crystal Structure of W26A mutant of anti-EGFR Centyrin P54AR4-83v2

PDB ID 5l2h

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