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Structural segments and residue propensities in protein-RNA interfaces: Comparison with protein-protein and protein-DNA complexes
The interface of a protein molecule that is involved in binding another protein, DNA or RNA has been characterized in terms of the number of unique secondary structural segments (SSSs), made up of stretches of helix, strand and non-regular (NR) regions. On average 10-11 segments define the protein i...
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Formato: | Texto |
Lenguaje: | English |
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Biomedical Informatics Publishing Group
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2561160/ https://www.ncbi.nlm.nih.gov/pubmed/18841236 |
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author | Biswas, Sumit Guharoy, Mainak Chakrabarti, Pinak |
author_facet | Biswas, Sumit Guharoy, Mainak Chakrabarti, Pinak |
author_sort | Biswas, Sumit |
collection | PubMed |
description | The interface of a protein molecule that is involved in binding another protein, DNA or RNA has been characterized in terms of the number of unique secondary structural segments (SSSs), made up of stretches of helix, strand and non-regular (NR) regions. On average 10-11 segments define the protein interface in protein-protein (PP) and protein-DNA (PD) complexes, while the number is higher (14) for protein-RNA (PR) complexes. While the length of helical segments in PP interaction increases with the interface area, this is not the case in PD and PR complexes. The propensities of residues to occur in the three types of secondary structural elements (SSEs) in the interface relative to the corresponding elements in the protein tertiary structures have been calculated. Arg, Lys, Asn, Tyr, His and Gln are preferred residues in PR complexes; in addition, Ser and Thr are also favoured in PD interfaces. |
format | Text |
id | pubmed-2561160 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Biomedical Informatics Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-25611602008-10-07 Structural segments and residue propensities in protein-RNA interfaces: Comparison with protein-protein and protein-DNA complexes Biswas, Sumit Guharoy, Mainak Chakrabarti, Pinak Bioinformation Hypothesis The interface of a protein molecule that is involved in binding another protein, DNA or RNA has been characterized in terms of the number of unique secondary structural segments (SSSs), made up of stretches of helix, strand and non-regular (NR) regions. On average 10-11 segments define the protein interface in protein-protein (PP) and protein-DNA (PD) complexes, while the number is higher (14) for protein-RNA (PR) complexes. While the length of helical segments in PP interaction increases with the interface area, this is not the case in PD and PR complexes. The propensities of residues to occur in the three types of secondary structural elements (SSEs) in the interface relative to the corresponding elements in the protein tertiary structures have been calculated. Arg, Lys, Asn, Tyr, His and Gln are preferred residues in PR complexes; in addition, Ser and Thr are also favoured in PD interfaces. Biomedical Informatics Publishing Group 2008-07-14 /pmc/articles/PMC2561160/ /pubmed/18841236 Text en © 2008 Biomedical Informatics Publishing Group This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited. |
spellingShingle | Hypothesis Biswas, Sumit Guharoy, Mainak Chakrabarti, Pinak Structural segments and residue propensities in protein-RNA interfaces: Comparison with protein-protein and protein-DNA complexes |
title | Structural segments and residue propensities in protein-RNA interfaces: Comparison with protein-protein and protein-DNA complexes |
title_full | Structural segments and residue propensities in protein-RNA interfaces: Comparison with protein-protein and protein-DNA complexes |
title_fullStr | Structural segments and residue propensities in protein-RNA interfaces: Comparison with protein-protein and protein-DNA complexes |
title_full_unstemmed | Structural segments and residue propensities in protein-RNA interfaces: Comparison with protein-protein and protein-DNA complexes |
title_short | Structural segments and residue propensities in protein-RNA interfaces: Comparison with protein-protein and protein-DNA complexes |
title_sort | structural segments and residue propensities in protein-rna interfaces: comparison with protein-protein and protein-dna complexes |
topic | Hypothesis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2561160/ https://www.ncbi.nlm.nih.gov/pubmed/18841236 |
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