1em4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{Theoretical_model}} | |||
==COMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENE== | ==COMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENE== | ||
<StructureSection load='1em4' size='340' side='right' caption='[[1em4]]' scene=''> | <StructureSection load='1em4' size='340' side='right' caption='[[1em4]]' scene=''> | ||
| Line 18: | Line 20: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Theoretical Model]] | |||
[[Category: Pellequer, J.-L]] | [[Category: Pellequer, J.-L]] | ||
[[Category: Roberts, V A]] | [[Category: Roberts, V A]] | ||
Revision as of 11:53, 11 February 2016
 |
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
|
| ||||||||||||||