Hydrogen/Deuterium Exchange Mass Spectrometry Reveals Specific Changes in the Local Flexibility of Plasminogen Activator Inhibitor 1 upon Binding to the Somatomedin B Domain of Vitronectin-Reference-Cited by-同舟云学术

Hydrogen/Deuterium Exchange Mass Spectrometry Reveals Specific Changes in the Local Flexibility of Plasminogen Activator Inhibitor 1 upon Binding to the Somatomedin B Domain of Vitronectin

Published:2012-10-04 Issue:41 Volume:51 Page:8256-8266
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Trelle Morten Beck¹,Hirschberg Daniel¹,Jansson Anna¹,Ploug Michael²,Roepstorff Peter¹,Andreasen Peter A.³,Jørgensen Thomas J. D.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark

2. Finsen Laboratory, Rigshospitalet and Biotech Research and Innovation Center (BRIC), Copenhagen Biocenter, Jagtvej 124, DK-2200 Copenhagen N, Denmark

3. Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10, DK-8000 Århus C, Denmark

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi3008998

Reference47 articles.

1. Serpin Structure, Mechanism, and Function

2. Biochemical properties of plasminogen activator inhibitor-1

3. The Molecular Basis for Anti-Proteolytic and Non-Proteolytic Functions of Plasminogen Activator Inhibitor Type-1: Roles of the Reactive Centre Loop, the Shutter Region, the Flexible Joint Region and the Small Serpin Fragment

4. Effects of Serpin Binding on the Target Proteinase: Global Stabilization, Localized Increased Structural Flexibility, and Conserved Hydrogen Bonding at the Active Site

5. The 2.1-Å Crystal Structure of Native Neuroserpin Reveals Unique Structural Elements That Contribute to Conformational Instability

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