Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
Nucleic Acids Res. 2010 Jan;38(Database issue):D283-7. doi: 10.1093/nar/gkp963. Epub 2009 Nov 11.
Most of the proteins in a cell assemble into complexes to carry out their function. In this work, we have created a new database (named ComSin) of protein structures in bound (complex) and unbound (single) states to provide a researcher with exhaustive information on structures of the same or homologous proteins in bound and unbound states. From the complete Protein Data Bank (PDB), we selected 24 910 pairs of protein structures in bound and unbound states, and identified regions of intrinsic disorder. For 2448 pairs, the proteins in bound and unbound states are identical, while 7129 pairs have sequence identity 90% or larger. The developed server enables one to search for proteins in bound and unbound states with several options including sequence similarity between the corresponding proteins in bound and unbound states, and validation of interaction interfaces of protein complexes. Besides that, through our web server, one can obtain necessary information for studying disorder-to-order and order-to-disorder transitions upon complex formation, and analyze structural differences between proteins in bound and unbound states. The database is available at http://antares.protres.ru/comsin/.
大多数细胞中的蛋白质都会组装成复合物来发挥其功能。在这项工作中，我们创建了一个新的数据库（名为 ComSin），其中包含结合（复合物）和未结合（单体）状态下的蛋白质结构，为研究人员提供关于结合和未结合状态下相同或同源蛋白质结构的详尽信息。我们从完整的蛋白质数据库（PDB）中选择了 24910 对结合和未结合状态的蛋白质结构，并确定了内在无序区域。对于 2448 对，结合态和未结合态的蛋白质是相同的，而 7129 对具有 90%或更高的序列同一性。开发的服务器允许用户使用几种选项搜索结合态和未结合态的蛋白质，包括结合态和未结合态相应蛋白质之间的序列相似性，以及蛋白质复合物相互作用界面的验证。除此之外，通过我们的网络服务器，用户可以获得研究复合物形成时无序到有序和有序到无序转变所需的信息，并分析结合态和未结合态蛋白质之间的结构差异。该数据库可在 http://antares.protres.ru/comsin/ 获得。
