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SInCRe-structural interactome computational resource for Mycobacterium tuberculosis

Metri, Rahul and Hariharaputran, Sridhar and Ramakrishnan, Gayatri and Anand, Praveen and Raghavender, Upadhyayula S and Ochoa-Montano, Bernardo and Higueruelo, Alicia P and Sowdhamini, Ramanathan and Chandra, Nagasuma R and Blundell, Tom L and Srinivasan, Narayanaswamy (2015) SInCRe-structural interactome computational resource for Mycobacterium tuberculosis. In: DATABASE-THE JOURNAL OF BIOLOGICAL DATABASES AND CURATION .

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Official URL: http://dx.doi.org/10.1093/database/bav060

Abstract

We have developed an integrated database for Mycobacterium tuberculosis H37Rv (Mtb) that collates information on protein sequences, domain assignments, functional annotation and 3D structural information along with protein-protein and protein-small molecule interactions. SInCRe (Structural Interactome Computational Resource) is developed out of CamBan (Cambridge and Bangalore) collaboration. The motivation for development of this database is to provide an integrated platform to allow easily access and interpretation of data and results obtained by all the groups in CamBan in the field of Mtb informatics. In-house algorithms and databases developed independently by various academic groups in CamBan are used to generate Mtb-specific datasets and are integrated in this database to provide a structural dimension to studies on tuberculosis. The SInCRe database readily provides information on identification of functional domains, genome-scale modelling of structures of Mtb proteins and characterization of the small-molecule binding sites within Mtb. The resource also provides structure-based function annotation, information on small-molecule binders including FDA (Food and Drug Administration)-approved drugs, protein-protein interactions (PPIs) and natural compounds that bind to pathogen proteins potentially and result in weakening or elimination of host-pathogen protein-protein interactions. Together they provide prerequisites for identification of off-target binding.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the OXFORD UNIV PRESS, GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAN
Department/Centre: Division of Biological Sciences > Biochemistry
Division of Biological Sciences > Molecular Biophysics Unit
Division of Physical & Mathematical Sciences > Mathematics
Depositing User: Id for Latest eprints
Date Deposited: 09 Oct 2015 05:27
Last Modified: 09 Oct 2015 05:27
URI: http://eprints.iisc.ac.in/id/eprint/52517

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