Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism
The metalloproteinase PAPP-A promotes insulin-like growth factor (IGF) signaling by cleavage of inhibitory IGF binding proteins. Here, the authors report the 3D structure of PAPP-A in complex with its endogenous inhibitor, stanniocalcin-2.
Main Authors: | , , , , , , , |
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Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2022-10-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-022-33698-8 |
Summary: | The metalloproteinase PAPP-A promotes insulin-like growth factor (IGF) signaling by cleavage of inhibitory IGF binding proteins. Here, the authors report the 3D structure of PAPP-A in complex with its endogenous inhibitor, stanniocalcin-2. |
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ISSN: | 2041-1723 |