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Inferred Biomolecular Interaction Server--a web server to analyze and predict protein interacting partners and binding sites.

Nucleic acids research | Jan 22, 2010

IBIS is the NCBI Inferred Biomolecular Interaction Server. This server organizes, analyzes and predicts interaction partners and locations of binding sites in proteins. IBIS provides annotations for different types of binding partners (protein, chemical, nucleic acid and peptides), and facilitates the mapping of a comprehensive biomolecular interaction network for a given protein query. IBIS reports interactions observed in experimentally determined structural complexes of a given protein, and at the same time IBIS infers binding sites/interacting partners by inspecting protein complexes formed by homologous proteins. Similar binding sites are clustered together based on their sequence and structure conservation. To emphasize biologically relevant binding sites, several algorithms are used for verification in terms of evolutionary conservation, biological importance of binding partners, size and stability of interfaces, as well as evidence from the published literature. IBIS is updated regularly and is freely accessible via http://www.ncbi.nlm.nih.gov/Structure/ibis/ibis.html.

Pubmed ID: 19843613 RIS Download

Mesh terms: Algorithms | Animals | Binding Sites | Catalytic Domain | Cluster Analysis | Computational Biology | Databases, Genetic | Databases, Protein | Humans | Information Storage and Retrieval | Internet | Protein Interaction Mapping | Protein Structure, Tertiary | Protein-Tyrosine Kinases | Software

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This is a list of tools and resources that we have found mentioned in this publication.

NCBI Structure: Cn3D

Cn3D is a helper application for your web browser that allows you to view 3-dimensional structures from NCBI''s Entrez retrieval service. Cn3D runs on Windows, Macintosh, and Unix. Cn3D simultaneously displays structure, sequence, and alignment, and now has powerful annotation and alignment editing features. Cn3D is a tool for visualization of three-dimensional structures with emphasis on interactive examination of sequence-structure relationships and superposition of geometrically similar structures. Can be used to display MMDB structures, superpositions of VAST related structures, and conserved core motifs identified in conserved domains.


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