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@ARTICLE{Mulnaes:873040,
author = {Mulnaes, Daniel and Porta, Nicola and Clemens, Rebecca and
Apanasenko, Irina and Reiners, Jens and Gremer, Lothar and
Neudecker, Philipp and Smits, Sander H. J. and Gohlke,
Holger},
title = {{T}op{M}odel: {T}emplate-based protein structure prediction
at low sequence identity using top-down consensus and deep
neural networks},
journal = {Journal of chemical theory and computation},
volume = {16},
number = {3},
issn = {1549-9626},
address = {Washington, DC},
reportid = {FZJ-2020-00491},
pages = {1953-1967},
year = {2020},
abstract = {Knowledge of protein structures is essential to understand
the proteins’ functions, evolution, dynamics, stabilities,
interactions, and for data-driven protein- or drug-design.
Yet, experimental structure determination rates are far
exceeded by that of next-generation sequencing.
Computational structure prediction seeks to alleviate this
problem, and the Critical Assessment of protein Structure
Prediction (CASP) has shown the value of consensus- and
meta-methods that utilize complementary algorithms. However,
traditionally, such methods employ majority voting during
template selection and model averaging during refinement,
which can drive the model away from the native fold if it is
underrepresented in the ensemble. Here, we present TopModel,
a fully automated meta-method for protein structure
prediction. In contrast to traditional consensus- and
meta-methods, TopModel uses top-down consensus and deep
neural networks to select templates and identify and correct
wrongly modeled regions. TopModel combines a broad range of
state-of-the-art methods for threading, alignment and model
quality estimation and provides a versatile work-flow and
toolbox for template-based structure prediction. TopModel
shows a superior template selection, alignment accuracy, and
model quality for template-based structure prediction on the
CASP10-12 datasets. TopModel was validated by prospective
predictions of the nisin resistance protein NSR protein from
S. agalactiae and LipoP from C. difficile, showing far
better agreement with experimental data than any of its
constituent primary predictors. These results, in general,
demonstrate the utility of TopModel for protein structure
prediction and, in particular, show how combining
computational structure prediction with sparse or
low-resolution experimental data can improve the final
model.},
cin = {JSC / NIC / ICS-6},
ddc = {610},
cid = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
I:(DE-Juel1)ICS-6-20110106},
pnm = {511 - Computational Science and Mathematical Methods
(POF3-511) / 551 - Functional Macromolecules and Complexes
(POF3-551) / Forschergruppe Gohlke $(hkf7_20170501)$},
pid = {G:(DE-HGF)POF3-511 / G:(DE-HGF)POF3-551 /
$G:(DE-Juel1)hkf7_20170501$},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:31967823},
UT = {WOS:000519337700048},
doi = {10.1021/acs.jctc.9b00825},
url = {https://juser.fz-juelich.de/record/873040},
}