Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II

Haloi et al. investigate the role of the hydrophobic N-terminus of hexokinase II (HKII) in their binding to mitochondrial VDAC1. They use a hybrid approach combining molecular and Brownian dynamics to show that HKII first inserts into the outer membrane of mitochondria (OMM) and then interacts with...

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Main Authors: Nandan Haloi, Po-Chao Wen, Qunli Cheng, Meiying Yang, Gayathri Natarajan, Amadou K. S. Camara, Wai-Meng Kwok, Emad Tajkhorshid
Format: Article
Language:English
Published: Nature Portfolio 2021-06-01
Series:Communications Biology
Online Access:https://doi.org/10.1038/s42003-021-02205-y
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author Nandan Haloi
Po-Chao Wen
Qunli Cheng
Meiying Yang
Gayathri Natarajan
Amadou K. S. Camara
Wai-Meng Kwok
Emad Tajkhorshid
author_facet Nandan Haloi
Po-Chao Wen
Qunli Cheng
Meiying Yang
Gayathri Natarajan
Amadou K. S. Camara
Wai-Meng Kwok
Emad Tajkhorshid
author_sort Nandan Haloi
collection DOAJ
description Haloi et al. investigate the role of the hydrophobic N-terminus of hexokinase II (HKII) in their binding to mitochondrial VDAC1. They use a hybrid approach combining molecular and Brownian dynamics to show that HKII first inserts into the outer membrane of mitochondria (OMM) and then interacts with VDAC1 on the cytosolic surface of OMM to form a binary complex.
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spelling doaj.art-9b0ee7be8cd74a3aaff79ae00681eddc2022-12-21T21:21:09ZengNature PortfolioCommunications Biology2399-36422021-06-014111210.1038/s42003-021-02205-yStructural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-IINandan Haloi0Po-Chao Wen1Qunli Cheng2Meiying Yang3Gayathri Natarajan4Amadou K. S. Camara5Wai-Meng Kwok6Emad Tajkhorshid7Theoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-ChampaignTheoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-ChampaignDepartment of Anesthesiology, Medical College of WisconsinDepartment of Anesthesiology, Medical College of WisconsinDepartment of Anesthesiology, Medical College of WisconsinDepartment of Anesthesiology, Medical College of WisconsinDepartment of Anesthesiology, Medical College of WisconsinTheoretical and Computational Biophysics Group, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-ChampaignHaloi et al. investigate the role of the hydrophobic N-terminus of hexokinase II (HKII) in their binding to mitochondrial VDAC1. They use a hybrid approach combining molecular and Brownian dynamics to show that HKII first inserts into the outer membrane of mitochondria (OMM) and then interacts with VDAC1 on the cytosolic surface of OMM to form a binary complex.https://doi.org/10.1038/s42003-021-02205-y
spellingShingle Nandan Haloi
Po-Chao Wen
Qunli Cheng
Meiying Yang
Gayathri Natarajan
Amadou K. S. Camara
Wai-Meng Kwok
Emad Tajkhorshid
Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II
Communications Biology
title Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II
title_full Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II
title_fullStr Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II
title_full_unstemmed Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II
title_short Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II
title_sort structural basis of complex formation between mitochondrial anion channel vdac1 and hexokinase ii
url https://doi.org/10.1038/s42003-021-02205-y
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