1em4: Difference between revisions
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[[ | ==COMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENE== | ||
<StructureSection load='1em4' size='340' side='right'caption='[[1em4]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EM4 FirstGlance]. <br> | |||
</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=1em4 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1em4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1em4 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Proteins can use aromatic side-chains to stabilize bound cationic ligands through cation-pi interactions. Here, we report the first example of the reciprocal process, termed pi-cation, in which a cationic protein side-chain stabilizes a neutral aromatic ligand. Site-directed mutagenesis revealed that an arginine side-chain located in the deep binding pocket of a monoclonal antibody (4D5) is essential for binding the neutral polynuclear aromatic hydrocarbon benzo[a]pyrene. This Arg was very likely selected for in the primary response, further underscoring the importance of the pi-cation interaction for ligand binding, which should be considered in protein analysis and design when ligands include aromatic groups. | |||
Stabilization of bound polycyclic aromatic hydrocarbons by a pi-cation interaction.,Pellequer JL, Zhao B, Kao HI, Bell CW, Li K, Li QX, Karu AE, Roberts VA J Mol Biol. 2000 Sep 22;302(3):691-9. PMID:10986127<ref>PMID:10986127</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1em4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Pellequer, J.-L]] | [[Category: Pellequer, J.-L]] | ||
[[Category: Roberts, V A]] | [[Category: Roberts, V A]] | ||
Latest revision as of 12:39, 21 July 2021
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COMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENECOMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENE
Structural highlights
Publication Abstract from PubMedProteins can use aromatic side-chains to stabilize bound cationic ligands through cation-pi interactions. Here, we report the first example of the reciprocal process, termed pi-cation, in which a cationic protein side-chain stabilizes a neutral aromatic ligand. Site-directed mutagenesis revealed that an arginine side-chain located in the deep binding pocket of a monoclonal antibody (4D5) is essential for binding the neutral polynuclear aromatic hydrocarbon benzo[a]pyrene. This Arg was very likely selected for in the primary response, further underscoring the importance of the pi-cation interaction for ligand binding, which should be considered in protein analysis and design when ligands include aromatic groups. Stabilization of bound polycyclic aromatic hydrocarbons by a pi-cation interaction.,Pellequer JL, Zhao B, Kao HI, Bell CW, Li K, Li QX, Karu AE, Roberts VA J Mol Biol. 2000 Sep 22;302(3):691-9. PMID:10986127[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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