Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex
10.1038/s41598-017-02219-9
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sg-nus-scholar.10635-1751862023-09-13T21:11:06Z Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex Kristal Kaan, H.Y Chan, S.W Tan, S.K.J Guo, F Lim, C.J Hong, W Song, H DUKE-NUS MEDICAL SCHOOL DEPT OF BIOCHEMISTRY DNA binding protein fusion protein muscle protein phosphoprotein protein binding signal transducing adaptor protein Taz protein, mouse Tead4 protein, mouse transcription factor Yap protein, mouse animal binding site chemistry metabolism molecular model mouse protein conformation protein domain protein multimerization structure activity relation Adaptor Proteins, Signal Transducing Animals Binding Sites DNA-Binding Proteins Mice Models, Molecular Muscle Proteins Phosphoproteins Protein Binding Protein Conformation Protein Interaction Domains and Motifs Protein Multimerization Recombinant Fusion Proteins Structure-Activity Relationship Transcription Factors 10.1038/s41598-017-02219-9 Scientific Reports 7 1 2035 2020-09-09T04:56:18Z 2020-09-09T04:56:18Z 2017 Article Kristal Kaan, H.Y, Chan, S.W, Tan, S.K.J, Guo, F, Lim, C.J, Hong, W, Song, H (2017). Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex. Scientific Reports 7 (1) : 2035. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-017-02219-9 20452322 https://scholarbank.nus.edu.sg/handle/10635/175186 Unpaywall 20200831 |
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DNA binding protein fusion protein muscle protein phosphoprotein protein binding signal transducing adaptor protein Taz protein, mouse Tead4 protein, mouse transcription factor Yap protein, mouse animal binding site chemistry metabolism molecular model mouse protein conformation protein domain protein multimerization structure activity relation Adaptor Proteins, Signal Transducing Animals Binding Sites DNA-Binding Proteins Mice Models, Molecular Muscle Proteins Phosphoproteins Protein Binding Protein Conformation Protein Interaction Domains and Motifs Protein Multimerization Recombinant Fusion Proteins Structure-Activity Relationship Transcription Factors |
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DNA binding protein fusion protein muscle protein phosphoprotein protein binding signal transducing adaptor protein Taz protein, mouse Tead4 protein, mouse transcription factor Yap protein, mouse animal binding site chemistry metabolism molecular model mouse protein conformation protein domain protein multimerization structure activity relation Adaptor Proteins, Signal Transducing Animals Binding Sites DNA-Binding Proteins Mice Models, Molecular Muscle Proteins Phosphoproteins Protein Binding Protein Conformation Protein Interaction Domains and Motifs Protein Multimerization Recombinant Fusion Proteins Structure-Activity Relationship Transcription Factors Kristal Kaan, H.Y Chan, S.W Tan, S.K.J Guo, F Lim, C.J Hong, W Song, H Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex |
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10.1038/s41598-017-02219-9 |
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DUKE-NUS MEDICAL SCHOOL |
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DUKE-NUS MEDICAL SCHOOL Kristal Kaan, H.Y Chan, S.W Tan, S.K.J Guo, F Lim, C.J Hong, W Song, H |
format |
Article |
author |
Kristal Kaan, H.Y Chan, S.W Tan, S.K.J Guo, F Lim, C.J Hong, W Song, H |
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Kristal Kaan, H.Y |
title |
Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex |
title_short |
Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex |
title_full |
Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex |
title_fullStr |
Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex |
title_full_unstemmed |
Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex |
title_sort |
crystal structure of taz-tead complex reveals a distinct interaction mode from that of yap-tead complex |
publishDate |
2020 |
url |
https://scholarbank.nus.edu.sg/handle/10635/175186 |
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1778169871506341888 |