1em4

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

COMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENECOMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENE

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1em4 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image