Reichmann Dana, Rahat Ofer, Cohen Mati, Neuvirth Hani, Schreiber Gideon
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Curr Opin Struct Biol. 2007 Feb;17(1):67-76. doi: 10.1016/j.sbi.2007.01.004. Epub 2007 Jan 18.
The formation of specific protein interactions plays a crucial role in most, if not all, biological processes, including signal transduction, cell regulation, the immune response and others. Recent advances in our understanding of the molecular architecture of protein-protein binding sites, which facilitates such diversity in binding affinity and specificity, are enabling us to address key questions. What is the amino acid composition of binding sites? What are interface hotspots? How are binding sites organized? What are the differences between tight and weak interacting complexes? How does water contribute to binding? Can the knowledge gained be translated into protein design? And does a universal code for binding exist, or is it the architecture and chemistry of the interface that enable diverse but specific binding solutions?
特异性蛋白质相互作用的形成在大多数（即便不是全部）生物过程中都起着关键作用，这些生物过程包括信号转导、细胞调控、免疫反应等。我们对蛋白质 - 蛋白质结合位点分子结构的理解取得了新进展，这有助于解释结合亲和力和特异性的多样性，使我们能够回答一些关键问题。结合位点的氨基酸组成是什么？界面热点有哪些？结合位点是如何组织的？紧密和弱相互作用复合物之间有何差异？水对结合有何作用？所获得的知识能否转化为蛋白质设计？是否存在通用的结合密码，还是界面的结构和化学性质促成了多样但特定的结合解决方案？
