ArticleCurrent protocols in bioinformatics2006
Comparative protein structure modeling using Modeller.
Article in Current protocols in bioinformatics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,404 papers.
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1,404 citing papers in PubMed.
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1,344 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
Functional characterization of a protein sequence is one of the most frequent problems in biology. This task is usually facilitated by accurate three-dimensional (3-D) structure of the studied protein. In the absence of an experimentally determined structure, comparative or homology modeling can sometimes provide a useful 3-D model for a protein that is related to at least one known protein structure. Comparative modeling predicts the 3-D structure of a given protein sequence (target) based primarily on its alignment to one or more proteins of known structure (templates). The prediction process consists of fold assignment, target-template alignment, model building, and model evaluation. This unit describes how to calculate comparative models using the program MODELLER and discusses all four steps of comparative modeling, frequently observed errors, and some applications. Modeling lactate dehydrogenase from Trichomonas vaginalis (TvLDH) is described as an example. The download and installation of the MODELLER software is also described.
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