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Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
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Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
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Personen und Körperschaften: | , , |
In: | Proceedings of the National Academy of Sciences, 101, 2004, 10, S. 3495-3497 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Proceedings of the National Academy of Sciences
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Schlagwörter: |
author_facet |
Liu, Yang Gerstein, Mark Engelman, Donald M. Liu, Yang Gerstein, Mark Engelman, Donald M. |
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author |
Liu, Yang Gerstein, Mark Engelman, Donald M. |
spellingShingle |
Liu, Yang Gerstein, Mark Engelman, Donald M. Proceedings of the National Academy of Sciences Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism Multidisciplinary |
author_sort |
liu, yang |
spelling |
Liu, Yang Gerstein, Mark Engelman, Donald M. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0307330101 <jats:p>Recombination of evolutionarily unrelated domains is a mechanism often used by evolution to produce variety in soluble proteins. By using a classification of polytopic transmembrane domains into families, we examined integral membrane proteins for evidence of this mechanism. Surprisingly, we found that domain recombination is not common for the transmembrane regions of membrane proteins, a majority of integral membrane proteins containing only a single transmembrane domain. We suggest that noncovalent oligomeric associations, which are common in membrane proteins, may provide an alternative source of evolutionary diversity.</jats:p> Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism Proceedings of the National Academy of Sciences |
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10.1073/pnas.0307330101 |
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Proceedings of the National Academy of Sciences, 2004 |
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Proceedings of the National Academy of Sciences, 2004 |
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2004 |
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Proceedings of the National Academy of Sciences |
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Proceedings of the National Academy of Sciences |
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title |
Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_unstemmed |
Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_full |
Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_fullStr |
Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_full_unstemmed |
Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_short |
Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_sort |
transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
topic |
Multidisciplinary |
url |
http://dx.doi.org/10.1073/pnas.0307330101 |
publishDate |
2004 |
physical |
3495-3497 |
description |
<jats:p>Recombination of evolutionarily unrelated domains is a mechanism often used by evolution to produce variety in soluble proteins. By using a classification of polytopic transmembrane domains into families, we examined integral membrane proteins for evidence of this mechanism. Surprisingly, we found that domain recombination is not common for the transmembrane regions of membrane proteins, a majority of integral membrane proteins containing only a single transmembrane domain. We suggest that noncovalent oligomeric associations, which are common in membrane proteins, may provide an alternative source of evolutionary diversity.</jats:p> |
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author | Liu, Yang, Gerstein, Mark, Engelman, Donald M. |
author_facet | Liu, Yang, Gerstein, Mark, Engelman, Donald M., Liu, Yang, Gerstein, Mark, Engelman, Donald M. |
author_sort | liu, yang |
container_issue | 10 |
container_start_page | 3495 |
container_title | Proceedings of the National Academy of Sciences |
container_volume | 101 |
description | <jats:p>Recombination of evolutionarily unrelated domains is a mechanism often used by evolution to produce variety in soluble proteins. By using a classification of polytopic transmembrane domains into families, we examined integral membrane proteins for evidence of this mechanism. Surprisingly, we found that domain recombination is not common for the transmembrane regions of membrane proteins, a majority of integral membrane proteins containing only a single transmembrane domain. We suggest that noncovalent oligomeric associations, which are common in membrane proteins, may provide an alternative source of evolutionary diversity.</jats:p> |
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imprint | Proceedings of the National Academy of Sciences, 2004 |
imprint_str_mv | Proceedings of the National Academy of Sciences, 2004 |
institution | DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15 |
issn | 0027-8424, 1091-6490 |
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language | English |
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spelling | Liu, Yang Gerstein, Mark Engelman, Donald M. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0307330101 <jats:p>Recombination of evolutionarily unrelated domains is a mechanism often used by evolution to produce variety in soluble proteins. By using a classification of polytopic transmembrane domains into families, we examined integral membrane proteins for evidence of this mechanism. Surprisingly, we found that domain recombination is not common for the transmembrane regions of membrane proteins, a majority of integral membrane proteins containing only a single transmembrane domain. We suggest that noncovalent oligomeric associations, which are common in membrane proteins, may provide an alternative source of evolutionary diversity.</jats:p> Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism Proceedings of the National Academy of Sciences |
spellingShingle | Liu, Yang, Gerstein, Mark, Engelman, Donald M., Proceedings of the National Academy of Sciences, Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism, Multidisciplinary |
title | Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_full | Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_fullStr | Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_full_unstemmed | Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_short | Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_sort | transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
title_unstemmed | Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism |
topic | Multidisciplinary |
url | http://dx.doi.org/10.1073/pnas.0307330101 |