Evidence map›Paper›PMID 34641789›Full record

ArticleBMC bioinformatics2021

CirPred, the first structure modeling and linker design system for circularly permuted proteins.

Teng-Ruei Chen, Yen-Cheng Lin, Yu-Wei Huang, Chih-Chieh Chen, Wei-Cheng Lo

Abstract read
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Article in BMC bioinformatics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

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3citing papers in PubMed
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3 · Its place in the literature

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3 citing papers in PubMed.

  1. Article
  2. Article
  3. SeqCP: A sequence-based algorithm for searching circularly permuted proteins.Computational and structural biotechnology journal · 2023
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5 · Who and what money

Authors and funding

5 authors.

Teng-Ruei Chen *Institute of Bioinformatics and Systems Biology, National Chiao Tung University, Hsinchu, Taiwan.
Yen-Cheng Lin *Department of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan.
Yu-Wei HuangInstitute of Bioinformatics and Systems Biology, National Chiao Tung University, Hsinchu, Taiwan.
Chih-Chieh ChenInstitute of Medical Science and Technology, National Sun Yat-sen University, Kaohsiung, Taiwan.
Wei-Cheng LoInstitute of Bioinformatics and Systems Biology, National Chiao Tung University, Hsinchu, Taiwan. WadeLo@nctu.edu.tw.ORCID http://orcid.org/0000-0001-8865-5113

Funding

Ministry of Science and Technology, Taiwan 101-2311-B-009-006-MY2Ministry of Science and Technology, Taiwan MOST-108-2221-E-110-061-MY2
6 · The paper itself

Abstract

backgroundThis work aims to help develop new protein engineering techniques based on a structural rearrangement phenomenon called circular permutation (CP), equivalent to connecting the native termini of a protein followed by creating new termini at another site. Although CP has been applied in many fields, its implementation is still costly because of inevitable trials and errors.

resultsHere we present CirPred, a structure modeling and termini linker design method for circularly permuted proteins. Compared with state-of-the-art protein structure modeling methods, CirPred is the only one fully capable of both circularly-permuted modeling and traditional co-linear modeling. CirPred performs well when the permutant shares low sequence identity with the native protein and even when the permutant adopts a different conformation from the native protein because of three-dimensional (3D) domain swapping. Linker redesign experiments demonstrated that the linker design algorithm of CirPred achieved subangstrom accuracy.

conclusionsThe CirPred system is capable of (1) predicting the structure of circular permutants, (2) designing termini linkers, (3) performing traditional co-linear protein structure modeling, and (4) identifying the CP-induced occurrence of 3D domain swapping. This method is supposed helpful for broadening the application of CP, and its web server is available at http://10.life.nctu.edu.tw/CirPred/ and http://lo.life.nctu.edu.tw/CirPred/ .

Indexed as

Protein EngineeringProteinsAlgorithmsProteinsCircular permutationProtein engineeringProtein structure modelingProtein structure prediction

Identifiers

PMID34641789
PMCPMC8513176

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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.