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Related Concept Videos

Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

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Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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System for Efficacy and Cytotoxicity Screening of Inhibitors Targeting Intracellular Mycobacterium tuberculosis
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System for Efficacy and Cytotoxicity Screening of Inhibitors Targeting Intracellular Mycobacterium tuberculosis

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SInCRe-structural interactome computational resource for Mycobacterium tuberculosis.

Rahul Metri1, Sridhar Hariharaputran2, Gayatri Ramakrishnan3

  • 1Department of Biochemistry and Indian Institute of Science Mathematics Initiative, Indian Institute of Science, Bangalore, India.

Database : the Journal of Biological Databases and Curation
|July 2, 2015
PubMed
Summary
This summary is machine-generated.

We created SInCRe, a database integrating Mycobacterium tuberculosis H37Rv data. This resource aids tuberculosis research by providing structural insights into protein interactions and drug targets.

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Area of Science:

  • Bioinformatics
  • Structural Biology
  • Computational Biology

Background:

  • Mycobacterium tuberculosis (Mtb) poses a significant global health challenge.
  • Understanding Mtb's molecular mechanisms requires integrated biological data.
  • Existing resources often lack comprehensive structural and interaction information.

Purpose of the Study:

  • To develop an integrated database, SInCRe (Structural Interactome Computational Resource), for Mycobacterium tuberculosis H37Rv.
  • To provide a unified platform for accessing and interpreting Mtb-specific data, including structural and interaction information.
  • To facilitate research in Mtb informatics by offering a structural dimension to existing datasets.

Main Methods:

  • Integration of in-house algorithms and databases from the CamBan collaboration.
  • Collating protein sequences, domain assignments, functional annotation, and 3D structural information.
  • Incorporating data on protein-protein interactions (PPIs) and protein-small molecule interactions.

Main Results:

  • SInCRe provides comprehensive data on Mtb proteins, including functional domains and genome-scale structural modeling.
  • The database characterizes small-molecule binding sites and offers structure-based function annotation.
  • Information on FDA-approved drugs, natural compounds, and potential off-target binding sites is available.

Conclusions:

  • SInCRe serves as a valuable resource for tuberculosis research by integrating diverse Mtb data.
  • The database enhances the interpretation of Mtb informatics studies through structural insights.
  • SInCRe facilitates the identification of potential drug targets and understanding of molecular interactions.