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The structure of the human presenilin-1 protein (orange) interacting with a fragment of one of its protein substrates, Notch (green). The catalytic aspartate sites are highlighted in blue spheres. Rendered using PyMOL from chains B and E of PDB: 6IDF​, a cryo-electron microscopy structure of the assembled gamma-secretase protein complex. In the construct used for the structure, D385 (aspartate on the left) was mutated to alanine; this residue has been modeled as an aspartate in this image for illustrative purposes.

Structural basis of Notch recognition by human gamma-secretase Yang, G., Zhou, R., Zhou, Q., Guo, X., Yan, C., Ke, M., Lei, J., Shi, Y.

(2019) Nature 565: 192-197. PubMed: 30598546 DOI: 10.1038/s41586-018-0813-8
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Author Opabinia regalis

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the structure of the human presenilin-1 protein

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27 January 2021

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current05:43, 28 January 2021Thumbnail for version as of 05:43, 28 January 2021800 × 800 (368 KB)Opabinia regalis{{Information |Description=The structure of the human presenilin-1 protein (orange) interacting with a fragment of one of its protein substrates, Notch (green). The catalytic aspartate sites are highlighted in blue spheres. Rendered using PyMOL from chains B and E of {{PDB|6IDF}}, a cryo-electron microscopy structure of the assembled gamma-secretase protein complex. Structural basis of Notch recognition by human gamma-secretase Yang, G., Zhou, R., Zhou, Q., Guo, X., Yan, C., Ke, M., Lei, J.,...

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