A framework for protein structure classification and identification of novel protein structures

<p>Abstract</p> <p>Background</p> <p>Protein structure classification plays a central role in understanding the function of a protein molecule with respect to all known proteins in a structure database. With the rapid increase in the number of new protein structures, th...

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Main Authors: Patel Jignesh M, Kim You
Format: Article
Language:English
Published: BMC 2006-10-01
Series:BMC Bioinformatics
Online Access:http://www.biomedcentral.com/1471-2105/7/456
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spelling doaj-9e2d38997e9e4a6e9209570aefd9a6f82020-11-25T02:27:31ZengBMCBMC Bioinformatics1471-21052006-10-017145610.1186/1471-2105-7-456A framework for protein structure classification and identification of novel protein structuresPatel Jignesh MKim You<p>Abstract</p> <p>Background</p> <p>Protein structure classification plays a central role in understanding the function of a protein molecule with respect to all known proteins in a structure database. With the rapid increase in the number of new protein structures, the need for <it>automated </it>and <it>accurate </it>methods for protein classification is increasingly important.</p> <p>Results</p> <p>In this paper we present a unified framework for protein structure classification and identification of novel protein structures. The framework consists of a set of components for comparing, classifying, and clustering protein structures. These components allow us to accurately classify proteins into known folds, to detect new protein folds, and to provide a way of clustering the new folds. In our evaluation with SCOP 1.69, our method correctly classifies 86.0%, 87.7%, and 90.5% of new domains at family, superfamily, and fold levels. Furthermore, for protein domains that belong to new domain families, our method is able to produce clusters that closely correspond to the new families in SCOP 1.69. As a result, our method can also be used to suggest new classification groups that contain novel folds.</p> <p>Conclusion</p> <p>We have developed a method called proCC for automatically classifying and clustering domains. The method is effective in classifying new domains and suggesting new domain families, and it is also very efficient. A web site offering access to proCC is freely available at <url>http://www.eecs.umich.edu/periscope/procc</url></p> http://www.biomedcentral.com/1471-2105/7/456
collection DOAJ
language English
format Article
sources DOAJ
author Patel Jignesh M
Kim You
spellingShingle Patel Jignesh M
Kim You
A framework for protein structure classification and identification of novel protein structures
BMC Bioinformatics
author_facet Patel Jignesh M
Kim You
author_sort Patel Jignesh M
title A framework for protein structure classification and identification of novel protein structures
title_short A framework for protein structure classification and identification of novel protein structures
title_full A framework for protein structure classification and identification of novel protein structures
title_fullStr A framework for protein structure classification and identification of novel protein structures
title_full_unstemmed A framework for protein structure classification and identification of novel protein structures
title_sort framework for protein structure classification and identification of novel protein structures
publisher BMC
series BMC Bioinformatics
issn 1471-2105
publishDate 2006-10-01
description <p>Abstract</p> <p>Background</p> <p>Protein structure classification plays a central role in understanding the function of a protein molecule with respect to all known proteins in a structure database. With the rapid increase in the number of new protein structures, the need for <it>automated </it>and <it>accurate </it>methods for protein classification is increasingly important.</p> <p>Results</p> <p>In this paper we present a unified framework for protein structure classification and identification of novel protein structures. The framework consists of a set of components for comparing, classifying, and clustering protein structures. These components allow us to accurately classify proteins into known folds, to detect new protein folds, and to provide a way of clustering the new folds. In our evaluation with SCOP 1.69, our method correctly classifies 86.0%, 87.7%, and 90.5% of new domains at family, superfamily, and fold levels. Furthermore, for protein domains that belong to new domain families, our method is able to produce clusters that closely correspond to the new families in SCOP 1.69. As a result, our method can also be used to suggest new classification groups that contain novel folds.</p> <p>Conclusion</p> <p>We have developed a method called proCC for automatically classifying and clustering domains. The method is effective in classifying new domains and suggesting new domain families, and it is also very efficient. A web site offering access to proCC is freely available at <url>http://www.eecs.umich.edu/periscope/procc</url></p>
url http://www.biomedcentral.com/1471-2105/7/456
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