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ProCMD: a database and 3D web resource for protein C mutants
BACKGROUND: Activated Protein C (ProC) is an anticoagulant plasma serine protease which also plays an important role in controlling inflammation and cell proliferation. Several mutations of the gene are associated with phenotypic functional deficiency of protein C, and with the risk of developing ve...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1885840/ https://www.ncbi.nlm.nih.gov/pubmed/17430555 http://dx.doi.org/10.1186/1471-2105-8-S1-S11 |
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author | D'Ursi, Pasqualina Marino, Francesca Caprera, Andrea Milanesi, Luciano Faioni, Elena M Rovida, Ermanna |
author_facet | D'Ursi, Pasqualina Marino, Francesca Caprera, Andrea Milanesi, Luciano Faioni, Elena M Rovida, Ermanna |
author_sort | D'Ursi, Pasqualina |
collection | PubMed |
description | BACKGROUND: Activated Protein C (ProC) is an anticoagulant plasma serine protease which also plays an important role in controlling inflammation and cell proliferation. Several mutations of the gene are associated with phenotypic functional deficiency of protein C, and with the risk of developing venous thrombosis. Structure prediction and computational analysis of the mutants have proven to be a valuable aid in understanding the molecular aspects of clinical thrombophilia. RESULTS: We have built a specialized relational database and a search tool for natural mutants of protein C. It contains 195 entries that include 182 missense and 13 stop mutations. A menu driven search engine allows the user to retrieve stored information for each variant, that include genetic as well as structural data and a multiple alignment highlighting the substituted position. Molecular models of variants can be visualized with interactive tools; PDB coordinates of the models are also available for further analysis. Furthermore, an automatic modelling interface allows the user to generate multiple alignments and 3D models of new variants. CONCLUSION: ProCMD is an up-to-date interactive mutant database that integrates phenotypical descriptions with functional and structural data obtained by computational approaches. It will be useful in the research and clinical fields to help elucidate the chain of events leading from a molecular defect to the related disease. It is available for academics at the URL . |
format | Text |
id | pubmed-1885840 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-18858402007-06-05 ProCMD: a database and 3D web resource for protein C mutants D'Ursi, Pasqualina Marino, Francesca Caprera, Andrea Milanesi, Luciano Faioni, Elena M Rovida, Ermanna BMC Bioinformatics Research BACKGROUND: Activated Protein C (ProC) is an anticoagulant plasma serine protease which also plays an important role in controlling inflammation and cell proliferation. Several mutations of the gene are associated with phenotypic functional deficiency of protein C, and with the risk of developing venous thrombosis. Structure prediction and computational analysis of the mutants have proven to be a valuable aid in understanding the molecular aspects of clinical thrombophilia. RESULTS: We have built a specialized relational database and a search tool for natural mutants of protein C. It contains 195 entries that include 182 missense and 13 stop mutations. A menu driven search engine allows the user to retrieve stored information for each variant, that include genetic as well as structural data and a multiple alignment highlighting the substituted position. Molecular models of variants can be visualized with interactive tools; PDB coordinates of the models are also available for further analysis. Furthermore, an automatic modelling interface allows the user to generate multiple alignments and 3D models of new variants. CONCLUSION: ProCMD is an up-to-date interactive mutant database that integrates phenotypical descriptions with functional and structural data obtained by computational approaches. It will be useful in the research and clinical fields to help elucidate the chain of events leading from a molecular defect to the related disease. It is available for academics at the URL . BioMed Central 2007-03-08 /pmc/articles/PMC1885840/ /pubmed/17430555 http://dx.doi.org/10.1186/1471-2105-8-S1-S11 Text en Copyright © 2007 D'Ursi et al; licensee BioMed Central Ltd. http://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) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research D'Ursi, Pasqualina Marino, Francesca Caprera, Andrea Milanesi, Luciano Faioni, Elena M Rovida, Ermanna ProCMD: a database and 3D web resource for protein C mutants |
title | ProCMD: a database and 3D web resource for protein C mutants |
title_full | ProCMD: a database and 3D web resource for protein C mutants |
title_fullStr | ProCMD: a database and 3D web resource for protein C mutants |
title_full_unstemmed | ProCMD: a database and 3D web resource for protein C mutants |
title_short | ProCMD: a database and 3D web resource for protein C mutants |
title_sort | procmd: a database and 3d web resource for protein c mutants |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1885840/ https://www.ncbi.nlm.nih.gov/pubmed/17430555 http://dx.doi.org/10.1186/1471-2105-8-S1-S11 |
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