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. 2003 Oct;4(10):937-8.
doi: 10.1038/sj.embor.embor946.

Subtleties among subtilases. The structural biology of Kex2 and furin-related prohormone convertases

Charles Brenner  1
Affiliations

Subtleties among subtilases. The structural biology of Kex2 and furin-related prohormone convertases

Charles Brenner. EMBO Rep. 2003 Oct.

Abstract

The structural biology of Kex2 and furin-related prohormone convertases

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Figures

Figure 1
Figure 1
Crystal structure of Kex2 protease. Stereo image with the amino terminus in orange, subtilisin domain in yellow, active-site residues in cyan, inhibitory peptide in blue, P-domain in purple, and C terminus in white. The pro-domain (Tangrea et al., 2002) would have extended from the N terminus across the active site, potenWtially to interact with the green surface of the P-domain. A site that could be engineered to test the hypothesis that the P-domain is dispensible after pro-domain cleavage is shown in red. Source data: Holyoak et al. (2003).
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