STRUCTURAL BIOLOGY OF MACROMOLECULAR STRUCTURE

这个实验室试图阐明管理 超分子络合物的组装和大分子的折叠， 以及那些作为病毒、细胞器和 其他高阶结构。在过去的一年里，我们发现了一个 蛋白质分子包装中的自由基偏离等价性 在噬菌体HK97的衣壳中。相同的蛋白质形成了两种 六角形和五角形，但五角形是循环对称的 五聚体，六角形不是循环对称的，而是由两个 相互侧向位移至少为20%的相对三聚体 埃斯特罗姆。在单纯疱疹病毒中，我们已经定位了小丰 衣壳蛋白，VP26(12kda)到六角形的外端 差分成像。它暴露的位置表明它的作用可能在于 将衣壳连接到周围的覆盖层。我们还研究了 几个主要的分子显示在外表面 病原菌百日咳杆菌。其中一个是丝状的 血凝素，是一种高免疫原性的黏附。FHA被发现假设 一种新型的50 nm长的单体发夹结构。ITS序列包含两个 长时间的19个残基重复序列与 富含亮氨酸的重复序列(LRR)存在于一组真核生物中 蛋白质，其中许多与细胞间黏附有关 现象。这一观察结果表明，FHA重复可能与 百日咳杆菌细胞与呼吸道的黏附。

This Laboratory seeks to elucidate the mechanisms that govern the assembly of supramolecular complexes and the folding of macromolecules, as well as those that underlie the synthesis of viruses, organelles, and other high order structures. In the past year, we have discovered a radical departure from equivalence in the packing of protein molecules in the capsid of bacteriophage HK97. The same protein forms both the hexons and pentons, but whereas the pentons are cyclically symmetric pentamers, the hexons are not cyclically symmetric, but consist of two apposed trimers with a mutual lateral displacement of at least 20 Angstroms. In herpes simplex virus, we have localized the small abundant capsid protein, VP26 (12 Kda) to the outer tips of hexons by quantitative difference imaging. Its exposed location suggests that its role may lie in coupling the capsid to the surrounding tegument. We have also studied several of the major molecules displayed at the outer surface of the pathogenic bacterium, Bordetella pertussis. One of these, filamentous hemagglutinin, is a high immunogenic adhesion. FHA was found to assume a novel 50nm-long monomeric hairpin structure. Its sequence contains two protracted runs of 19-residue repeats which strongly resemble the leucine-rich repeats (LRRs) that are present in a set of eukaryotic proteins, many of which have been implicated in intercellular adhesion phenomena. This observation suggests that FHA repeats may be involved in the adhesion of B. pertussis cells to the respiratory tract.