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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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Detalles Bibliográficos
Autor principal: Kumar, Suresh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2011
Materias:
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.
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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