tailieunhanh - Báo cáo y học: "CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationship"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Critical Care giúp cho các bạn có thêm kiến thức về ngành y học đề tài: CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships. | Open Access Method CPSARST an efficient circular permutation search tool applied to the detection of novel protein structural relationships Wei-Cheng Lo and Ping-Chiang Lyu Address Institute of Bioinformatics and Structural Biology National Tsing Hua University Hsinchu 30013 Taiwan. Correspondence Ping-Chiang Lyu. Email pclyu@ Published 18 January 2008 Genome Biology 2008 9 R1 I doi 186 gb-2008-9-1-r11 The electronic version of this article is the complete one and can be found online at http 2008 9 1 R11 Received 11 September 2007 Revised 19 November 2007 Accepted l8 January 2008 2008 Lo 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 Circular permutation of a protein can be visualized as if the original amino- and carboxyl termini were linked and new ones created elsewhere. It has been well-documented that circular permutants usually retain native structures and biological functions. Here we report CPSARST Circular Permutation Search Aided by Ramachandran Sequential Transformation to be an efficient database search tool. In this post-genomics era when the amount of protein structural data is increasing exponentially it provides a new way to rapidly detect novel relationships among proteins. Background Circular permutation CP in a protein structure is the rearrangement of the amino acid sequence such that the amino-and carboxy-terminal regions are interchanged 1 2 . It can be visualized as if the original termini of the polypeptide were linked and new ones created elsewhere 3 4 . Since the first observation of naturally occurring circular permutations in plant lectins 5 a substantial number of natural examples have been reported including some bacterial p-glucanases .