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首页> 外文期刊>Proteins: Structure, Function, and Genetics >Antibody recognition of chiral surfaces. Structural models of antibody complexes with leucine-leucine-tyrosine crystal surfaces.
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Antibody recognition of chiral surfaces. Structural models of antibody complexes with leucine-leucine-tyrosine crystal surfaces.

机译：手性表面的抗体识别。具有亮氨酸-亮氨酸-酪氨酸晶体表面的抗体复合物的结构模型。

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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.
机译：基于两种抗体的识别域构建分子模型，针对（L）亮氨酸-（L）亮氨酸-（L）酪氨酸的晶体产生并选择该抗体。一种具有立体选择性和对映选择性的抗体模型揭示了与公认晶体表面惊人的化学和结构互补性。该抗体的对映选择性结合是由于相对于其对映异构体（ L）Leu-（L）Leu-（L）Tyr晶体面。立体选择性差而对映选择性差的第二种抗体的建模和对接表明结合是基于静电相互作用。抗体-晶体复合物的对接模型为实验结果提供了理论依据，同时展示了建模技术的强大功能，可以应对详细描述抗体-抗原相互作用的挑战。

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