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Title |
Modeling and structural analysis of human Guanine nucleotide-binding protein-like 3, nucleostemin |
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Authors |
Farinaz Nazmi1,2, Mohammad Amin Moosavi1,3*, Marveh Rahmati3, Mohammad Ali Hoessinpour-Feizi2 |
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Affiliation |
1Department of Molecular Medicine, Institute of Medical biotechnology, National Institute for genetic Engineering and biotechnology, Tehran, Iran; 2Department of Zoology, Faculty of Natural Science, The University of Tabriz, Iran; 3Hematology and Oncology Research Center, Tabriz University of medical Science, Tabriz, Iran
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a-moosavi@nigeb.ac.ir; *Corresponding author
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Article Type |
Hypothesis
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Date |
Received June 02 2015; Revised June 28, 2015; Accepted June 29, 2015; Published July 31, 2015
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Abstract |
Human GNL3 (nucleostemin) is a recently discovered nucleolar protein with pivotal functions in maintaining genomic integrity and determining cell fates of various normal and cancerous stem cells. Recent reports suggest that targeting this GTP-binding protein may have therapeutic value in cancer. Although, sequence analyzing revealed that nucleostemin (NS) comprises 5 permuted GTP-binding motifs, a crystal structure for this protein is missing at Protein Data Bank (PDB). Obviously, any attempt for predicting of NS structure can further our knowledge on its functional sites and subsequently designing molecular inhibitors. Herein, we used bioinformatics tools and could model 262 amino acids of NS (132-393 aa). Initial models were built by MODELLER, refined with Scwrl4 program, and validated with ProsA and Jcsc databases as well as PSVS software. Then, the best quality model was chosen for motif and domain analyzing by Pfam, PROSITE and PRINTS. The final model was visualized by vmd program. This predicted model may pave the way for next studies regarding ligand binding states and interaction sites as well as screening of databases for potential inhibitors.
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Citation |
Nazmi et al.
Bioinformation 11(7): 353-358 (2015) |
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Edited by |
P Kangueane
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ISSN |
0973-2063
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Publisher |
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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.
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