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Extending CATH: increasing coverage of the protein structure universe and linking structure with function
CATH version 3.3 (class, architecture, topology, homology) contains 128 688 domains, 2386 homologous superfamilies and 1233 fold groups, and reflects a major focus on classifying structural genomics (SG) structures and transmembrane proteins, both of which are likely to add structural novelty to the...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013636/ https://www.ncbi.nlm.nih.gov/pubmed/21097779 http://dx.doi.org/10.1093/nar/gkq1001 |
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author | Cuff, Alison L. Sillitoe, Ian Lewis, Tony Clegg, Andrew B. Rentzsch, Robert Furnham, Nicholas Pellegrini-Calace, Marialuisa Jones, David Thornton, Janet Orengo, Christine A. |
author_facet | Cuff, Alison L. Sillitoe, Ian Lewis, Tony Clegg, Andrew B. Rentzsch, Robert Furnham, Nicholas Pellegrini-Calace, Marialuisa Jones, David Thornton, Janet Orengo, Christine A. |
author_sort | Cuff, Alison L. |
collection | PubMed |
description | CATH version 3.3 (class, architecture, topology, homology) contains 128 688 domains, 2386 homologous superfamilies and 1233 fold groups, and reflects a major focus on classifying structural genomics (SG) structures and transmembrane proteins, both of which are likely to add structural novelty to the database and therefore increase the coverage of protein fold space within CATH. For CATH version 3.4 we have significantly improved the presentation of sequence information and associated functional information for CATH superfamilies. The CATH superfamily pages now reflect both the functional and structural diversity within the superfamily and include structural alignments of close and distant relatives within the superfamily, annotated with functional information and details of conserved residues. A significantly more efficient search function for CATH has been established by implementing the search server Solr (http://lucene.apache.org/solr/). The CATH v3.4 webpages have been built using the Catalyst web framework. |
format | Text |
id | pubmed-3013636 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-30136362011-01-03 Extending CATH: increasing coverage of the protein structure universe and linking structure with function Cuff, Alison L. Sillitoe, Ian Lewis, Tony Clegg, Andrew B. Rentzsch, Robert Furnham, Nicholas Pellegrini-Calace, Marialuisa Jones, David Thornton, Janet Orengo, Christine A. Nucleic Acids Res Articles CATH version 3.3 (class, architecture, topology, homology) contains 128 688 domains, 2386 homologous superfamilies and 1233 fold groups, and reflects a major focus on classifying structural genomics (SG) structures and transmembrane proteins, both of which are likely to add structural novelty to the database and therefore increase the coverage of protein fold space within CATH. For CATH version 3.4 we have significantly improved the presentation of sequence information and associated functional information for CATH superfamilies. The CATH superfamily pages now reflect both the functional and structural diversity within the superfamily and include structural alignments of close and distant relatives within the superfamily, annotated with functional information and details of conserved residues. A significantly more efficient search function for CATH has been established by implementing the search server Solr (http://lucene.apache.org/solr/). The CATH v3.4 webpages have been built using the Catalyst web framework. Oxford University Press 2011-01 2010-11-19 /pmc/articles/PMC3013636/ /pubmed/21097779 http://dx.doi.org/10.1093/nar/gkq1001 Text en © The Author(s) 2010. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Cuff, Alison L. Sillitoe, Ian Lewis, Tony Clegg, Andrew B. Rentzsch, Robert Furnham, Nicholas Pellegrini-Calace, Marialuisa Jones, David Thornton, Janet Orengo, Christine A. Extending CATH: increasing coverage of the protein structure universe and linking structure with function |
title | Extending CATH: increasing coverage of the protein structure universe and linking structure with function |
title_full | Extending CATH: increasing coverage of the protein structure universe and linking structure with function |
title_fullStr | Extending CATH: increasing coverage of the protein structure universe and linking structure with function |
title_full_unstemmed | Extending CATH: increasing coverage of the protein structure universe and linking structure with function |
title_short | Extending CATH: increasing coverage of the protein structure universe and linking structure with function |
title_sort | extending cath: increasing coverage of the protein structure universe and linking structure with function |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3013636/ https://www.ncbi.nlm.nih.gov/pubmed/21097779 http://dx.doi.org/10.1093/nar/gkq1001 |
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