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Calcium affinity of human α-actinin 1
Due to alternative splicing, the human ACTN1 gene codes for three different transcripts of α-actinin; one isoform that is expressed only in the brain and two with a more general expression pattern. The sequence difference is located to the C-terminal domains and the EF-hand motifs. Therefore, any fu...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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PeerJ Inc.
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4435478/ https://www.ncbi.nlm.nih.gov/pubmed/26020004 http://dx.doi.org/10.7717/peerj.944 |
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author | Backman, Lars |
author_facet | Backman, Lars |
author_sort | Backman, Lars |
collection | PubMed |
description | Due to alternative splicing, the human ACTN1 gene codes for three different transcripts of α-actinin; one isoform that is expressed only in the brain and two with a more general expression pattern. The sequence difference is located to the C-terminal domains and the EF-hand motifs. Therefore, any functional or structural distinction should involve this part of the protein. To investigate this further, the calcium affinities of these three isoforms of α-actinin 1 have been determined by isothermal calorimetry. |
format | Online Article Text |
id | pubmed-4435478 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | PeerJ Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-44354782015-05-27 Calcium affinity of human α-actinin 1 Backman, Lars PeerJ Biochemistry Due to alternative splicing, the human ACTN1 gene codes for three different transcripts of α-actinin; one isoform that is expressed only in the brain and two with a more general expression pattern. The sequence difference is located to the C-terminal domains and the EF-hand motifs. Therefore, any functional or structural distinction should involve this part of the protein. To investigate this further, the calcium affinities of these three isoforms of α-actinin 1 have been determined by isothermal calorimetry. PeerJ Inc. 2015-05-07 /pmc/articles/PMC4435478/ /pubmed/26020004 http://dx.doi.org/10.7717/peerj.944 Text en © 2015 Backman http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. |
spellingShingle | Biochemistry Backman, Lars Calcium affinity of human α-actinin 1 |
title | Calcium affinity of human α-actinin 1 |
title_full | Calcium affinity of human α-actinin 1 |
title_fullStr | Calcium affinity of human α-actinin 1 |
title_full_unstemmed | Calcium affinity of human α-actinin 1 |
title_short | Calcium affinity of human α-actinin 1 |
title_sort | calcium affinity of human α-actinin 1 |
topic | Biochemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4435478/ https://www.ncbi.nlm.nih.gov/pubmed/26020004 http://dx.doi.org/10.7717/peerj.944 |
work_keys_str_mv | AT backmanlars calciumaffinityofhumanaactinin1 |