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Title

Homology modeling and consensus protein disorder prediction of human filamin

 

Authors

Suresh Kumar*

 

Affiliation

Department of Bioinformatics, School of Biotechnology and Health Sciences, Karunya University, Coimbatore - 641114, Tamil Nadu, India;

 

Email

sureshbio@gmail.com; *Corresponding author

 

Article Type

Hypothesis

 

Date

Received July 12, 2011; Accepted July 14, 2011; Published August 02, 2011

 

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 understand its role in function.

 

Keywords

human filamin, Calponin CH domain, Ig-like domain, homology modeling, protein disorder

 

Citation

Kumar. Bioinformation 6(10): 366-369 (2011)
 

Edited by

P Kangueane

 

ISSN

0973-2063

 

Publisher

Biomedical Informatics

 

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.