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Homology modeling and consensus protein disorder prediction of human filamin
Filamins are dimeric actin-binding proteins participating in the organization of the actin-based cytoskeleton. Their modular domain organization is made up of an N-terminal actin-binding domain composed of two CH domains followed by flexible rod regions that consist of 24 Ig-like domains. Homology m...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Biomedical Informatics
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3163912/ https://www.ncbi.nlm.nih.gov/pubmed/21904422 |
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author | Kumar, Suresh |
author_facet | Kumar, Suresh |
author_sort | Kumar, Suresh |
collection | PubMed |
description | Filamins are dimeric actin-binding proteins participating in the organization of the actin-based cytoskeleton. Their modular domain organization is made up of an N-terminal actin-binding domain composed of two CH domains followed by flexible rod regions that consist of 24 Ig-like domains. Homology modeling was used to model human filamin using Modeller 9v5. The resulting model assessed by Verify 3D and PROCHECK showed that the final model is reliable. The conformational disorder prediction of human filamin residues were also mapped on the validated structure of human filamin. Prediction of protein disorder in filamin structures will help understand its role in function. |
format | Online Article Text |
id | pubmed-3163912 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
spelling | pubmed-31639122011-09-08 Homology modeling and consensus protein disorder prediction of human filamin Kumar, Suresh Bioinformation Hypothesis Filamins are dimeric actin-binding proteins participating in the organization of the actin-based cytoskeleton. Their modular domain organization is made up of an N-terminal actin-binding domain composed of two CH domains followed by flexible rod regions that consist of 24 Ig-like domains. Homology modeling was used to model human filamin using Modeller 9v5. The resulting model assessed by Verify 3D and PROCHECK showed that the final model is reliable. The conformational disorder prediction of human filamin residues were also mapped on the validated structure of human filamin. Prediction of protein disorder in filamin structures will help understand its role in function. Biomedical Informatics 2011-08-02 /pmc/articles/PMC3163912/ /pubmed/21904422 Text en © 2011 Biomedical Informatics 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 Kumar, Suresh Homology modeling and consensus protein disorder prediction of human filamin |
title | Homology modeling and consensus protein disorder prediction of human filamin |
title_full | Homology modeling and consensus protein disorder prediction of human filamin |
title_fullStr | Homology modeling and consensus protein disorder prediction of human filamin |
title_full_unstemmed | Homology modeling and consensus protein disorder prediction of human filamin |
title_short | Homology modeling and consensus protein disorder prediction of human filamin |
title_sort | homology modeling and consensus protein disorder prediction of human filamin |
topic | Hypothesis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3163912/ https://www.ncbi.nlm.nih.gov/pubmed/21904422 |
work_keys_str_mv | AT kumarsuresh homologymodelingandconsensusproteindisorderpredictionofhumanfilamin |