DIFFRACTION FROM CRYSTALS OF MULTIMODULE FIBRONECTIN CELL ADHESION FRAGMENTS

细胞表面受体对细胞外配体的识别 （整合素）对于细胞粘附、迁移和追踪至关重要， 可能是肿瘤细胞的转移性扩散。 这种认识是 部分由精氨酸-甘氨酸-天冬氨酸序列介导， 胞外蛋白质 我们最近克隆并表达了更大的 每个包含模块FN 11110的多模块片段。 我们有 结晶了其中三块碎片 这些碎片很重要 结构的候选人，以揭示三维组织的RGD网站 以及相邻结构域中的协同位点， 整合素识别和分子的粘附功能。 需要同步辐射来收集这些重原子数据 小水晶

Recognition of extracellular ligands by cell surface receptors (integrins) is critical for cell adhesion, migration and tracking and perhaps the metastatic spread of tumor cells. This recognition is mediated in part by an arginine-glycine-aspartic acid sequence in extracellular proteins. We have recently cloned and expressed larger multimodule fragments that each contain the module FN 11110. We have crystallized three of these fragments. These fragments are important structural candidates to reveal the 3D organization of the RGD site and synergistic sites in adjacent domains that are required for integrin recognition and adhesive function of the molecule. Synchrotron radiation is needed to collect heavy atom data from these small crystals.