
@article {908,
	title = {Enriching the annotation of Mycobacterium tuberculosis H37Rv proteome using remote homology detection approaches: insights into structure and function.},
	journal = {Tuberculosis (Edinb)},
	volume = {95},
	year = {2015},
	month = {2015 Jan},
	pages = {14-25},
	abstract = {<p>The availability of the genome sequence of Mycobacterium tuberculosis H37Rv has encouraged determination of large numbers of protein structures and detailed definition of the biological information encoded therein; yet, the functions of many proteins in M. tuberculosis remain unknown. The emergence of multidrug resistant strains makes it a priority to exploit recent advances in homology recognition and structure prediction to re-analyse its gene products. Here we report the structural and functional characterization of gene products encoded in the M. tuberculosis genome, with the help of sensitive profile-based remote homology search and fold recognition algorithms resulting in an enhanced annotation of the proteome where 95\% of the M. tuberculosis proteins were identified wholly or partly with information on structure or function. New information includes association of 244 proteins with 205 domain families and a separate set of new association of folds to 64 proteins. Extending structural information across uncharacterized protein families represented in the M. tuberculosis proteome, by determining superfamily relationships between families of known and unknown structures, has contributed to an enhancement in the knowledge of structural content. In retrospect, such superfamily relationships have facilitated recognition of probable structure and/or function for several uncharacterized protein families, eventually aiding recognition of probable functions for homologous proteins corresponding to such families. Gene products unique to mycobacteria for which no functions could be identified are 183. Of these 18 were determined to be M. tuberculosis specific. Such pathogen-specific proteins are speculated to harbour virulence factors required for pathogenesis. A re-annotated proteome of M. tuberculosis, with greater completeness of annotated proteins and domain assigned regions, provides a valuable basis for experimental endeavours designed to obtain a better understanding of pathogenesis and to accelerate the process of drug target discovery.</p>
},
	keywords = {Hydrolases, Mycobacterium tuberculosis, Protein Structure, Tertiary, Proteome, Sequence Analysis, Protein, Structural Homology, Protein},
	issn = {1873-281X},
	doi = {10.1016/j.tube.2014.10.009},
	author = {Ramakrishnan, Gayatri and Ochoa-Monta{\~n}o, Bernardo and Raghavender, Upadhyayula S and Mudgal, Richa and Joshi, Adwait G and Chandra, Nagasuma R and Sowdhamini, Ramanathan and Blundell, Tom L and Srinivasan, Narayanaswamy}
}
@article {1002,
	title = {SInCRe-structural interactome computational resource for Mycobacterium tuberculosis.},
	journal = {Database (Oxford)},
	volume = {2015},
	year = {2015},
	month = {2015},
	pages = {bav060},
	abstract = {<p>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.</p>
},
	issn = {1758-0463},
	doi = {10.1093/database/bav060},
	author = {Metri, Rahul and Hariharaputran, Sridhar and Ramakrishnan, Gayatri and Anand, Praveen and Raghavender, Upadhyayula S and Ochoa-Monta{\~n}o, Bernardo and Higueruelo, Alicia P and Sowdhamini, Ramanathan and Chandra, Nagasuma R and Blundell, Tom L and Srinivasan, Narayanaswamy}
}
