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CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships

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...

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Detalles Bibliográficos
Autores principales: Lo, Wei-Cheng, Lyu, Ping-Chiang
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2395249/
https://www.ncbi.nlm.nih.gov/pubmed/18201387
http://dx.doi.org/10.1186/gb-2008-9-1-r11
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author Lo, Wei-Cheng
Lyu, Ping-Chiang
author_facet Lo, Wei-Cheng
Lyu, Ping-Chiang
author_sort Lo, Wei-Cheng
collection PubMed
description 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.
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spelling pubmed-23952492008-05-29 CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships Lo, Wei-Cheng Lyu, Ping-Chiang Genome Biol Method 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. BioMed Central 2008-01-18 /pmc/articles/PMC2395249/ /pubmed/18201387 http://dx.doi.org/10.1186/gb-2008-9-1-r11 Text en Copyright © 2008 Lo et al.; licensee BioMed Central Ltd. https://creativecommons.org/licenses/by/2.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0 (https://creativecommons.org/licenses/by/2.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Method
Lo, Wei-Cheng
Lyu, Ping-Chiang
CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships
title CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships
title_full CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships
title_fullStr CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships
title_full_unstemmed CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships
title_short CPSARST: an efficient circular permutation search tool applied to the detection of novel protein structural relationships
title_sort cpsarst: an efficient circular permutation search tool applied to the detection of novel protein structural relationships
topic Method
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2395249/
https://www.ncbi.nlm.nih.gov/pubmed/18201387
http://dx.doi.org/10.1186/gb-2008-9-1-r11
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