Fig. 1: Modular structure of the 1546-residue PAPP-A (pappalysin-1) subunit. | Nature Communications

Fig. 1: Modular structure of the 1546-residue PAPP-A (pappalysin-1) subunit.

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

Fig. 1

Approximate domain boundaries and the cysteine residue responsible for PAPP-A dimerization are indicated. Note that two Lin12-Notch repeat (LNR) modules (LNR1-2) are inserted into the catalytic domain (CD), and a third (LNR3) is present as part of the C domain. No sequence similarity has been detected for the central region of 500 residues, which is designated M. The short consensus repeats (SCR) are also known as CCP domains. PAPP-A promotes IGF signaling by binding via SCR3-4 to glycosaminoglycan (GAG), present at the cell surface. This allows proteolytic release of IGF in close proximity to the IGF receptor.

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