Hunte Carola, Michel Hartmut
Max-Planck-Institut für Biophysik, Abt Molekulare Membranbiologie, Heinrich-Hoffmann-Strasse 7, D-60528 Frankfurt am Main, Germany.
Curr Opin Struct Biol. 2002 Aug;12(4):503-8. doi: 10.1016/s0959-440x(02)00354-8.
X-ray structures of three different membrane proteins in complex with antibody fragments have been published. The binding of Fv or Fab fragments enlarges the hydrophilic part of integral membrane proteins, thereby providing additional surface for crystal contacts and space for the detergent micelle. In all reported cases, antibody binding was either essential for the crystallisation of the membrane protein or it substantially improved the diffraction quality of the crystals. Antibody-fragment-mediated crystallisation appears to be a valuable tool in particular for membrane proteins with very small hydrophilic or flexible domains.
三种不同膜蛋白与抗体片段复合物的X射线结构已发表。Fv或Fab片段的结合扩大了整合膜蛋白的亲水部分,从而为晶体接触提供了额外的表面,并为去污剂胶束提供了空间。在所有报道的案例中,抗体结合对于膜蛋白的结晶要么是必不可少的,要么它显著提高了晶体的衍射质量。抗体片段介导的结晶似乎是一种有价值的工具,尤其适用于具有非常小的亲水或柔性结构域的膜蛋白。