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 |
| _version_ | 1811249896789901312 |
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| author | Sara Dam Kobberø Michael Gajhede Osman Asghar Mirza Søren Kløverpris Troels Rønn Kjær Jakob Hauge Mikkelsen Thomas Boesen Claus Oxvig |
| author_facet | Sara Dam Kobberø Michael Gajhede Osman Asghar Mirza Søren Kløverpris Troels Rønn Kjær Jakob Hauge Mikkelsen Thomas Boesen Claus Oxvig |
| author_sort | Sara Dam Kobberø |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T15:55:32Z |
| format | Article |
| id | doaj.art-dd1bab3f3f344221a1bcddc8c4635e2f |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-12T15:55:32Z |
| publishDate | 2022-10-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-dd1bab3f3f344221a1bcddc8c4635e2f2022-12-22T03:26:24ZengNature PortfolioNature Communications2041-17232022-10-0113111610.1038/s41467-022-33698-8Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanismSara Dam Kobberø0Michael Gajhede1Osman Asghar Mirza2Søren Kløverpris3Troels Rønn Kjær4Jakob Hauge Mikkelsen5Thomas Boesen6Claus Oxvig7Department of Molecular Biology and Genetics, Aarhus UniversityDepartment of Drug Design and Pharmacology, University of CopenhagenDepartment of Drug Design and Pharmacology, University of CopenhagenDepartment of Molecular Biology and Genetics, Aarhus UniversityDepartment of Molecular Biology and Genetics, Aarhus UniversityDepartment of Molecular Biology and Genetics, Aarhus UniversityInterdisciplinary Nanoscience Center, Aarhus UniversityDepartment of Molecular Biology and Genetics, Aarhus UniversityThe 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.https://doi.org/10.1038/s41467-022-33698-8 |
| spellingShingle | Sara Dam Kobberø Michael Gajhede Osman Asghar Mirza Søren Kløverpris Troels Rønn Kjær Jakob Hauge Mikkelsen Thomas Boesen Claus Oxvig Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism Nature Communications |
| title | Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism |
| title_full | Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism |
| title_fullStr | Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism |
| title_full_unstemmed | Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism |
| title_short | Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism |
| title_sort | structure of the proteolytic enzyme papp a with the endogenous inhibitor stanniocalcin 2 reveals its inhibitory mechanism |
| url | https://doi.org/10.1038/s41467-022-33698-8 |
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