Homology modeling and consensus protein disorder prediction of human filamin |
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Authors: | Kumar Suresh |
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Affiliation: | Department of Bioinformatics, School of Biotechnology and Health Sciences, Karunya University, Coimbatore - 641114, Tamil Nadu, India |
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Abstract: | 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 structural biologists to find suitable targets to be analyzed and for understanding protein function. |
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Keywords: | human filamin Calponin CH domain Ig-like domain homology modeling protein disorder |
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