Evidence map›Paper›PMID 31341084›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Assembling multidomain protein structures through analogous global structural alignments.

Xiaogen Zhou, Jun Hu, Chengxin Zhang, Guijun Zhang, Yang Zhang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

63 citing papers in PubMed.

  1. MultilevelCurrent research in structural biology · 2026
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3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Xiaogen ZhouCollege of Information Engineering, Zhejiang University of Technology, 310023 HangZhou, China.ORCID 0000-0001-6839-1923
Jun HuCollege of Information Engineering, Zhejiang University of Technology, 310023 HangZhou, China.
Chengxin ZhangDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109.
Guijun ZhangCollege of Information Engineering, Zhejiang University of Technology, 310023 HangZhou, China; zgj@zjut.edu.cn zhng@umich.edu.
Yang ZhangDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109; zgj@zjut.edu.cn zhng@umich.edu.ORCID 0000-0002-2739-1916

Funding

Structure-based functional annotation of microbial genomesR01AI134678 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Lydia Petra Freddolino, SCOTT J. HULTGREN · 2018 to 2026
$6.5M
I-TASSER based atomic-level protein structure predictionR01GM083107 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2008 to 2019
$3.5M
Template-based docking refinement approach to protein-protein structure modelingR01GM116960 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2016 to 2019
$1.4M
NIAID NIH HHS R01 AI134678NIGMS NIH HHS R01 GM083107NIGMS NIH HHS R01 GM116960
6 · The paper itself

Abstract

Most proteins exist with multiple domains in cells for cooperative functionality. However, structural biology and protein folding methods are often optimized for single-domain structures, resulting in a rapidly growing gap between the improved capability for tertiary structure determination and high demand for multidomain structure models. We have developed a pipeline, termed DEMO, for constructing multidomain protein structures by docking-based domain assembly simulations, with interdomain orientations determined by the distance profiles from analogous templates as detected through domain-level structure alignments. The pipeline was tested on a comprehensive benchmark set of 356 proteins consisting of 2-7 continuous and discontinuous domains, for which DEMO generated models with correct global fold (TM-score > 0.5) for 86% of cases with continuous domains and for 100% of cases with discontinuous domain structures, starting from randomly oriented target-domain structures. DEMO was also applied to reassemble multidomain targets in the CASP12 and CASP13 experiments using domain structures excised from the top server predictions, where the full-length DEMO models showed a significantly improved quality over the original server models. Finally, sparse restraints of mass spectrometry-generated cross-linking data and cryo-EM density maps are incorporated into DEMO, resulting in improvements in the average TM-score by 6.3% and 12.5%, respectively. The results demonstrate an efficient approach to assembling multidomain structures, which can be easily used for automated, genome-scale multidomain protein structure assembly.

Indexed as

Cross-Linking ReagentsCryoelectron MicroscopyDatabases, ProteinModels, MolecularProtein DomainsProteinsSoftwareCross-Linking ReagentsProteinsdomain assemblymultidomain proteinmultidomain template recognitionprotein structure prediction

Identifiers

PMID31341084
PMCPMC6689945

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.