Figure 7
Residues R660, Y661, and Y665 align as a cluster on the surface of ADAMTS13 MDTCS. The recent ADAMTS13 DTCS crystal structure (3GHM)44 and previously generated model of the ADAMTS13 metalloprotease domain30 were aligned to create a model of the ADAMTS13 MDTCS domains (PyMOL; DeLano Scientific). The metalloprotease domain is shown in yellow (MP) with the catalytic zinc ion indicated in magenta. The disintegrin-like domain (Dis) is in green and residues R349 and D350 that have previously been established as exosite for VWF are shown in dark green. The TSP1, cysteine-rich (Cys), and spacer domains are shown in blue, pink, and orange, respectively. Residues R660, Y661, and Y665 are highlighted by the box to show where they are located on the surface of MDTCS. The alternative representation of the side chains of these residues shows that they align in this structure to form a cluster that is surface exposed.

Residues R660, Y661, and Y665 align as a cluster on the surface of ADAMTS13 MDTCS. The recent ADAMTS13 DTCS crystal structure (3GHM)44  and previously generated model of the ADAMTS13 metalloprotease domain30  were aligned to create a model of the ADAMTS13 MDTCS domains (PyMOL; DeLano Scientific). The metalloprotease domain is shown in yellow (MP) with the catalytic zinc ion indicated in magenta. The disintegrin-like domain (Dis) is in green and residues R349 and D350 that have previously been established as exosite for VWF are shown in dark green. The TSP1, cysteine-rich (Cys), and spacer domains are shown in blue, pink, and orange, respectively. Residues R660, Y661, and Y665 are highlighted by the box to show where they are located on the surface of MDTCS. The alternative representation of the side chains of these residues shows that they align in this structure to form a cluster that is surface exposed.

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