The N-terminal autoinhibitory module of the A1 domain in von Willebrand factor stabilizes the mechanosensor catch bond

Author:

Zhao Yunduo Charles12ORCID,Wang Haoqing13,Wang Yao14,Lou Jizhong5ORCID,Ju Lining Arnold12367ORCID

Affiliation:

1. School of Biomedical Engineering, Faculty of Engineering, The University of Sydney, Darlington, NSW 2008, Australia

2. Charles Perkins Centre, The University of Sydney, Camperdown, NSW 2006, Australia

3. Heart Research Institute, Newtown, NSW 2042, Australia

4. Cellular and Genetic Medicine Unit, School of Medical Sciences, University of New South Wales, NSW 2052, Australia

5. Key Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China

6. The University of Sydney Nano Institute (Sydney Nano), The University of Sydney, Camperdown, NSW 2006, Australia

7. Coulter Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, GA 30332, USA

Abstract

The N-AIM of VWF-A1 forms a Rotini-like structure, therefore partially autoinhibit VWF-A1–GPIbα interaction. The N-AIM acts as a defending sword to protect and stabilize the VWF-A1 structure under harsh environments.

Funder

Ramaciotti Foundations

Australian Academy of Science

National Heart Foundation of Australia

Australian Research Council

National Health and Medical Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry,Chemistry (miscellaneous)

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