Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Minireview cung cấp cho các bạn kiến thức về ngành y đề tài: Evolutionary conservation of domain-domain interactions. | Open Access Evolutionary conservation of domain-domain interactions Zohar Itzhaki Eyal Akiva Yael Altuvia and Hanah Margalit Address Department of Molecular Genetics and Biotechnology Faculty of Medicine The Hebrew University of Jerusalem Jerusalem 91120 Israel. Correspondence Hanah Margalit. Email hanah@ Published 21 December 2006 Received 16 August 2006 Genome Biology 2006 7 R125 doi gb-2006-7- 12-r 125 The electronic version of this article is the complete one and can be found online at http 2006 7 12 R125 Revised 6 November 2006 Accepted 21 December 2006 2006 Itzhaki et al. licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background Recently there has been much interest in relating domain-domain interactions DDIs to protein-protein interactions PPIs and vice versa in an attempt to understand the molecular basis of PPIs. Results Here we map structurally derived DDIs onto the cellular PPI networks of different organisms and demonstrate that there is a catalog of domain pairs that is used to mediate various interactions in the cell. We show that these DDIs occur frequently in protein complexes and that homotypic interactions of a domain with itself are abundant. A comparison of the repertoires of DDIs in the networks of Escherichia coli Saccharomyces cerevisiae Caenorhabditis elegans Drosophila melanogaster and Homo sapiens shows that many DDIs are evolutionarily conserved. Conclusion Our results indicate that different organisms use the same building blocks for PPIs suggesting that the functionality of many domain pairs in mediating protein interactions is maintained in evolution. Background Many proteins are constructed of domains which are their main functional and .
