Comparative protein structure modeling of genes and genomes

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dc.catalogadoraba
dc.contributor.authorMartí-Renom, M. A.
dc.contributor.authorStuart, A. C.
dc.contributor.authorFiser, A.
dc.contributor.authorSánchez, R.
dc.contributor.authorMelo Ledermann, Francisco Javier
dc.contributor.authorSali, A.
dc.date.accessioned2025-02-06T20:12:31Z
dc.date.available2025-02-06T20:12:31Z
dc.date.issued2000
dc.description.abstractComparative modeling predicts the three-dimensional 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. The number of protein sequences that can be modeled and the accuracy of the predictions are increasing steadily because of the growth in the number of known protein structures and because of the improvements in the modeling software. Further advances are necessary in recognizing weak sequence–structure similarities, aligning sequences with structures, modeling of rigid body shifts, distortions, loops and side chains, as well as detecting errors in a model. Despite these problems, it is currently possible to model with useful accuracy significant parts of approximately one third of all known protein sequences. The use of individual comparative models in biology is already rewarding and increasingly widespread. A major new challenge for comparative modeling is the integration of it with the torrents of data from genome sequencing projects as well as from functional and structural genomics. In particular, there is a need to develop an automated, rapid, robust, sensitive, and accurate comparative modeling pipeline applicable to whole genomes. Such large-scale modeling is likely to encourage new kinds of applications for the many resulting models, based on their large number and completeness at the level of the family, organism, or functional network.
dc.format.extent35 páginas
dc.fuente.origenSIPA
dc.identifier.doi10.1146/annurev.biophys.29.1.291
dc.identifier.eissn1936-1238
dc.identifier.issn1936-122X
dc.identifier.pubmedid10940251
dc.identifier.urihttps://doi.org/10.1146/annurev.biophys.29.1.291
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/102202
dc.identifier.wosidWOS:000088492300011
dc.information.autorucFacultad de Ciencias Biológicas; Melo Ledermann, Francisco Javier; 0000-0002-0424-5991; 82342
dc.language.isoen
dc.nota.accesocontenido parcial
dc.pagina.final325
dc.pagina.inicio291
dc.revistaAnnual review of biophysics and biomolecular structure
dc.rightsacceso restringido
dc.subjectProtein structure prediction
dc.subjectFold assignment
dc.subjectAlignment
dc.subjectHomology modeling
dc.subjectModel evaluation
dc.subjectFully automated modeling
dc.subjectStructural genomics
dc.subject.ddc570
dc.subject.deweyBiologíaes_ES
dc.titleComparative protein structure modeling of genes and genomes
dc.typeartículo
dc.volumen29
sipa.codpersvinculados82342
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