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Open AccessJournal ArticleDOI

Dali server: conservation mapping in 3D

Liisa Holm, +1 more
- 01 Jul 2010 - 
- Vol. 38, pp 545-549
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TLDR
The key purpose of interactive analysis is to check whether conserved residues line up in multiple structural alignments and how Conserved residues and ligands cluster together in multiple structure superimpositions.
Abstract
Our web site (http://ekhidna.biocenter.helsinki.fi/dali_server) runs the Dali program for protein structure comparison. The web site consists of three parts: (i) the Dali server compares newly solved structures against structures in the Protein Data Bank (PDB), (ii) the Dali database allows browsing precomputed structural neighbourhoods and (iii) the pairwise comparison generates suboptimal alignments for a pair of structures. Each part has its own query form and a common format for the results page. The inputs are either PDB identifiers or novel structures uploaded by the user. The results pages are hyperlinked to aid interactive analysis. The web interface is simple and easy to use. The key purpose of interactive analysis is to check whether conserved residues line up in multiple structural alignments and how conserved residues and ligands cluster together in multiple structure superimpositions. In favourable cases, protein structure comparison can lead to evolutionary discoveries not detected by sequence analysis.

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References
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Journal ArticleDOI

Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions

TL;DR: The present paper describes the SSM algorithm of protein structure comparison in three dimensions, which includes an original procedure of matching graphs built on the protein's secondary-structure elements, followed by an iterative three-dimensional alignment of protein backbone Calpha atoms.
Journal ArticleDOI

Mapping the Protein Universe

TL;DR: An exhaustive all-on-all shape comparison provides a map of physical attractor regions in the abstract shape space of proteins, with implications for the processes of protein folding and evolution.
Journal ArticleDOI

ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures

TL;DR: This new version of ConSurf includes an empirical Bayesian method for scoring conservation, which is more accurate than the maximum-likelihood method that was used in the earlier release and includes a measure of confidence for the inferred amino acid conservation scores.
Journal ArticleDOI

Surprising similarities in structure comparison

TL;DR: New structural comparison methods, developed in the past two years, increasingly offer this opportunity to structural and molecular biologists in general, and several groups seem to have converged on quite similar approaches with respect to both fast search algorithms and the identification of statistically significant similarities.
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