Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.
URL: http://topofit.ilyinlab.org/topofit/topofit_db.php
Proper Citation: TOPOFIT Database (RRID:SCR_006936)
Description: THIS RESOURCE IS NO LONGER IN SERVICE, documented on August 26, 2016. The T-DB contains millions of structural alignments between all proteins in the PDB as of July 2005 found by the TOPOFIT method. Structural neighbors to the query protein structure can be retrieved by the PDB code and chain id. Pairwise or multiple structural alignments can be visualized in 3D with the FRIEND software. In the TOPOFIT method, similarity of protein structures is analyzed using three-dimensional Delaunay triangulation patterns derived from backbone representation. It has been found that structurally related proteins have a common spatial invariant part, a set of tetrahedrons, mathematically described as a common spatial sub-graph volume of the three-dimensional contact graph derived from Delaunay tessellation (DT). Based on this property of protein structures we present a novel common volume superimposition (TOPOFIT) method to produce structural alignments of proteins. The superimposition of the DT patterns allows one to uniquely identify a common number of equivalent residues in the structural alignment, in other words, TOPOFIT identifies a feature point on the RMSD/Ne curve, a topomax point, until which two structures correspond to each other including backbone and inter-residue contacts, while the growing number of mismatches between the DT patterns occurs at larger RMSD (Ne) after topomax point. The topomax point is present in all alignments from different protein structural classes; therefore, the TOPOFIT method identifies common, invariant structural parts between proteins. The TOPOFIT method adds new opportunities for the comparative analysis of protein structures and for more detailed studies on understanding the molecular principles of tertiary structure organization and functionality. It helps to detect conformational changes, topological differences in variable parts, which are particularly important for studies of variations in active/binding sites and protein classification.
Synonyms: T-DB
Resource Type: data or information resource, database
Expand Allhas parent organization |
We found {{ ctrl2.mentions.all_count }} mentions in open access literature.
We have not found any literature mentions for this resource.
We are searching literature mentions for this resource.
Most recent articles:
{{ mention._source.dc.creators[0].familyName }} {{ mention._source.dc.creators[0].initials }}, et al. ({{ mention._source.dc.publicationYear }}) {{ mention._source.dc.title }} {{ mention._source.dc.publishers[0].name }}, {{ mention._source.dc.publishers[0].volume }}({{ mention._source.dc.publishers[0].issue }}), {{ mention._source.dc.publishers[0].pagination }}. (PMID:{{ mention._id.replace('PMID:', '') }})
A list of researchers who have used the resource and an author search tool
A list of researchers who have used the resource and an author search tool. This is available for resources that have literature mentions.
No rating or validation information has been found for TOPOFIT Database.
No alerts have been found for TOPOFIT Database.
Source: SciCrunch Registry