IDDI: integrated domain-domain interaction and protein interaction analysis system

<p>Abstract</p> <p>Background</p> <p>Deciphering protein-protein interaction (PPI) in domain level enriches valuable information about binding mechanism and functional role of interacting proteins. The 3D structures of complex proteins are reliable source of domain-doma...

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Main Authors: Kim Yul, Min Bumki, Yi Gwan-Su
Format: Article
Language:English
Published: BMC 2012-06-01
Series:Proteome Science
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spelling doaj-9db057e26dae4d9b9d6e466ddfa337f12020-11-24T23:07:57ZengBMCProteome Science1477-59562012-06-0110Suppl 1S910.1186/1477-5956-10-S1-S9IDDI: integrated domain-domain interaction and protein interaction analysis systemKim YulMin BumkiYi Gwan-Su<p>Abstract</p> <p>Background</p> <p>Deciphering protein-protein interaction (PPI) in domain level enriches valuable information about binding mechanism and functional role of interacting proteins. The 3D structures of complex proteins are reliable source of domain-domain interaction (DDI) but the number of proven structures is very limited. Several resources for the computationally predicted DDI have been generated but they are scattered in various places and their prediction show erratic performances. A well-organized PPI and DDI analysis system integrating these data with fair scoring system is necessary.</p> <p>Method</p> <p>We integrated three structure-based DDI datasets and twenty computationally predicted DDI datasets and constructed an interaction analysis system, named IDDI, which enables to browse protein and domain interactions with their relationships. To integrate heterogeneous DDI information, a novel scoring scheme is introduced to determine the reliability of DDI by considering the prediction scores of each DDI and the confidence levels of each prediction method in the datasets, and independencies between predicted datasets. In addition, we connected this DDI information to the comprehensive PPI information and developed a unified interface for the interaction analysis exploring interaction networks at both protein and domain level.</p> <p>Result</p> <p>IDDI provides 204,705 DDIs among total 7,351 Pfam domains in the current version. The result presents that total number of DDIs is increased eight times more than that of previous studies. Due to the increment of data, 50.4% of PPIs could be correlated with DDIs which is more than twice of previous resources. Newly designed scoring scheme outperformed the previous system in its accuracy too. User interface of IDDI system provides interactive investigation of proteins and domains in interactions with interconnected way. A specific example is presented to show the efficiency of the systems to acquire the comprehensive information of target protein with PPI and DDI relationships. IDDI is freely available at <url>http://pcode.kaist.ac.kr/iddi/</url>.</p>
collection DOAJ
language English
format Article
sources DOAJ
author Kim Yul
Min Bumki
Yi Gwan-Su
spellingShingle Kim Yul
Min Bumki
Yi Gwan-Su
IDDI: integrated domain-domain interaction and protein interaction analysis system
Proteome Science
author_facet Kim Yul
Min Bumki
Yi Gwan-Su
author_sort Kim Yul
title IDDI: integrated domain-domain interaction and protein interaction analysis system
title_short IDDI: integrated domain-domain interaction and protein interaction analysis system
title_full IDDI: integrated domain-domain interaction and protein interaction analysis system
title_fullStr IDDI: integrated domain-domain interaction and protein interaction analysis system
title_full_unstemmed IDDI: integrated domain-domain interaction and protein interaction analysis system
title_sort iddi: integrated domain-domain interaction and protein interaction analysis system
publisher BMC
series Proteome Science
issn 1477-5956
publishDate 2012-06-01
description <p>Abstract</p> <p>Background</p> <p>Deciphering protein-protein interaction (PPI) in domain level enriches valuable information about binding mechanism and functional role of interacting proteins. The 3D structures of complex proteins are reliable source of domain-domain interaction (DDI) but the number of proven structures is very limited. Several resources for the computationally predicted DDI have been generated but they are scattered in various places and their prediction show erratic performances. A well-organized PPI and DDI analysis system integrating these data with fair scoring system is necessary.</p> <p>Method</p> <p>We integrated three structure-based DDI datasets and twenty computationally predicted DDI datasets and constructed an interaction analysis system, named IDDI, which enables to browse protein and domain interactions with their relationships. To integrate heterogeneous DDI information, a novel scoring scheme is introduced to determine the reliability of DDI by considering the prediction scores of each DDI and the confidence levels of each prediction method in the datasets, and independencies between predicted datasets. In addition, we connected this DDI information to the comprehensive PPI information and developed a unified interface for the interaction analysis exploring interaction networks at both protein and domain level.</p> <p>Result</p> <p>IDDI provides 204,705 DDIs among total 7,351 Pfam domains in the current version. The result presents that total number of DDIs is increased eight times more than that of previous studies. Due to the increment of data, 50.4% of PPIs could be correlated with DDIs which is more than twice of previous resources. Newly designed scoring scheme outperformed the previous system in its accuracy too. User interface of IDDI system provides interactive investigation of proteins and domains in interactions with interconnected way. A specific example is presented to show the efficiency of the systems to acquire the comprehensive information of target protein with PPI and DDI relationships. IDDI is freely available at <url>http://pcode.kaist.ac.kr/iddi/</url>.</p>
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