Proteins: Structure, Function and Bioinformatics 2004-06-01

Antibody recognition of chiral surfaces. Structural models of antibody complexes with leucine-leucine-tyrosine crystal surfaces.

Merav Geva, Miriam Eisenstein, Lia Addadi

文献索引：Proteins 55(4) , 862-73, (2004)

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摘要

Molecular models are built of the recognition domains of two antibodies, which are raised and selected against crystals of (L)leucine-(L)leucine-(L)tyrosine. The model of one antibody, which is stereo- and enantioselective, reveals astounding chemical and structural complementarity to the recognized crystal surface. The enantioselective binding of this antibody is explained by the significantly fewer chemical interactions arising in the complex, after docking of the antibody to the (D)Leu-(D)Leu-(D)Tyr crystal face, relative to its enantiomer, the (L)Leu-(L)Leu-(L)Tyr crystal face. The modeling and docking of the second antibody, which is poorly stereoselective and is not enantioselective, indicates that binding is based on electrostatic interactions. The docking models of the antibody-crystal complexes provide a rationale for the experimental results while demonstrating the power of modeling techniques to meet the challenge of describing antibody-antigen interactions in detail.Copyright 2004 Wiley-Liss, Inc.