Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism

Sara Dam Kobberø; Michael Gajhede; Osman Asghar Mirza; Søren Kløverpris; Troels Rønn Kjær; Jakob Hauge Mikkelsen; Thomas Boesen; Claus Oxvig

doi:10.1038/s41467-022-33698-8

Nature Communications (Oct 2022)

Structure of the proteolytic enzyme PAPP-A with the endogenous inhibitor stanniocalcin-2 reveals its inhibitory mechanism

Sara Dam Kobberø,
Michael Gajhede,
Osman Asghar Mirza,
Søren Kløverpris,
Troels Rønn Kjær,
Jakob Hauge Mikkelsen,
Thomas Boesen,
Claus Oxvig

Affiliations

Sara Dam Kobberø: Department of Molecular Biology and Genetics, Aarhus University
Michael Gajhede: Department of Drug Design and Pharmacology, University of Copenhagen
Osman Asghar Mirza: Department of Drug Design and Pharmacology, University of Copenhagen
Søren Kløverpris: Department of Molecular Biology and Genetics, Aarhus University
Troels Rønn Kjær: Department of Molecular Biology and Genetics, Aarhus University
Jakob Hauge Mikkelsen: Department of Molecular Biology and Genetics, Aarhus University
Thomas Boesen: Interdisciplinary Nanoscience Center, Aarhus University
Claus Oxvig: Department of Molecular Biology and Genetics, Aarhus University

DOI: https://doi.org/10.1038/s41467-022-33698-8
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 16

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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