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. 2021 Jan 21;41(3):1092–1104. doi: 10.1161/ATVBAHA.120.315030

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© 2021 The Authors.

Arteriosclerosis, Thrombosis, and Vascular Biology is published on behalf of the American Heart Association, Inc., by Wolters Kluwer Health, Inc. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution, and reproduction in any medium, provided that the original work is properly cited.

This article is made available via the PMC Open Access Subset for unrestricted re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the COVID-19 pandemic or until permissions are revoked in writing. Upon expiration of these permissions, PMC is granted a perpetual license to make this article available via PMC and Europe PMC, consistent with existing copyright protections.

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Figure 6. — Atomic force microscopy topography images of interactions between GPVI (glycoprotein VI) and fibrinogen. The fibrinogen molecules are highlighted using 3 black circles for its D-E-D structure. The disordered fibrinogen αC-regions are visible as flexible appendices with reduced height (and therefore reduced brightness) from the D-region or close to the E-region. A–D, GPVI monomer are indicated with cyan circles; (E–H) GPVI dimer are indicated with magenta circles. The αC-region of fibrinogen involved in GPVI binding is highlighted with triangles. Two structural isoforms of GPVI dimer were observed: one as a large single-domain globular protein and the other as an elongated shape or as 2 domains with similar sizes closely associated with each other.