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Investigating architecture and structure-function relationships in cold shock DNA-binding domain family using structural genomics-based approach
Jamia Millia Islamia, Ctr Interdisciplinary Res Basic Sci, New Delhi 110025, India.
Amity Univ Noida, Amity Inst Neuropsychol & Neurosci, Noida, UP, India.
Jamia Millia Islamia, Ctr Interdisciplinary Res Basic Sci, New Delhi 110025, India;King Saud Univ, Dept Pharmacogmosy, Coll Pharm, Riyadh 11451, Saudi Arabia.
King Saud Univ, Dept Pharmacogmosy, Coll Pharm, Riyadh 11451, Saudi Arabia.
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2019 (Engelska)Ingår i: International Journal of Biological Macromolecules, ISSN 0141-8130, E-ISSN 1879-0003, Vol. 133, s. 484-494Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Oligonucleotide/oligosaccharide-binding fold (OB-fold) plays a major role in the regulation of central dogma of life via binding though DNA and RNA. The OB-fold domains are diverse in nature and present in large number of proteins with verities of molecular functions. Here, we have investigated the distribution of sequence, structure and repeats of cold shock DNA-binding proteins (CSDB), a member of OB-fold, in all three kingdoms to establish functional relationships. The CSDB is consists of 30 domains with a major contribution of S1 (>110,601 sequences), S12 (>23,760 sequences), S17 (>14,833 sequences) and S28e (>1615 sequence) domains. These domains are largely found in bacteria (70-90%). The number of S1 domain repeats in eukaryota varies from 1 to 15 and are well-correlated with the protein size. The molecular function analysis suggests that a large number of repeats in the S1 domain are involved in diverse molecular functions in bacteria and eukaryotes. In-depth structure analysis of Si, S12, S17 and S28e domain-containing proteins of the OB-fold family provides a reasonable basis to understand the relationship of size and number of repeats with the corresponding molecular functions.

Ort, förlag, år, upplaga, sidor
ELSEVIER SCIENCE BV , 2019. Vol. 133, s. 484-494
Nyckelord [en]
OB-fold, Nucleic acid-binding superfamily, Cold shock DNA-binding proteins, RNA-binding proteins, Structural genomics, Molecular evolution
Nationell ämneskategori
Biokemi och molekylärbiologi
Identifikatorer
URN: urn:nbn:se:uu:diva-390782DOI: 10.1016/j.ijbiomac.2019.04.135ISI: 000472685700053PubMedID: 31005689OAI: oai:DiVA.org:uu-390782DiVA, id: diva2:1343277
Tillgänglig från: 2019-08-16 Skapad: 2019-08-16 Senast uppdaterad: 2019-08-16Bibliografiskt granskad

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