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TitleCryo-EM structure of human PAPP-A2 and mechanism of substrate recognition.
Journal, issue, pagesCommun Chem, Vol. 6, Issue 1, Page 234, Year 2023
Publish dateOct 28, 2023
AuthorsJanani Sridar / Amirhossein Mafi / Russell A Judge / Jun Xu / Kailyn A Kong / John C K Wang / Vincent S Stoll / Georgios Koukos / Reyna J Simon / Dan Eaton / Matthew Bratkowski / Qi Hao /
PubMed AbstractPregnancy-Associated Plasma Protein A isoforms, PAPP-A and PAPP-A2, are metalloproteases that cleave insulin-like growth factor binding proteins (IGFBPs) to modulate insulin-like growth factor ...Pregnancy-Associated Plasma Protein A isoforms, PAPP-A and PAPP-A2, are metalloproteases that cleave insulin-like growth factor binding proteins (IGFBPs) to modulate insulin-like growth factor signaling. The structures of homodimeric PAPP-A in complex with IGFBP5 anchor peptide, and inhibitor proteins STC2 and proMBP have been recently reported. Here, we present the single-particle cryo-EM structure of the monomeric, N-terminal LG, MP, and the M1 domains (with the exception of LNR1/2) of human PAPP-A2 to 3.13 Å resolution. Our structure together with functional studies provides insight into a previously reported patient mutation that inactivates PAPP-A2 in a distal region of the protein. Using a combinational approach, we suggest that PAPP-A2 recognizes IGFBP5 in a similar manner as PAPP-A and show that PAPP-A2 cleaves IGFBP5 less efficiently due to differences in the M2 domain. Overall, our studies characterize the cleavage mechanism of IGFBP5 by PAPP-A2 and shed light onto key differences with its paralog PAPP-A.
External linksCommun Chem / PubMed:37898658 / PubMed Central
MethodsEM (single particle)
Resolution3.13 Å
Structure data

40571

8sl1

EMDB-40571, PDB-8sl1:
Cryo-EM structure of PAPP-A2
Method: EM (single particle) / Resolution: 3.13 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsHYDROLASE / PEPTIDE BINDING PROTEIN / Protease / zinc binding / growth factor signaling / peptide binding

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