Pregnancy-associated plasma protein-A (PAPP-A) is a zymogen. It is cleaved to form an active protease that degrades insulin-like growth factor binding proteins (IGFBPs). The three-dimensional (3D) structure of PAPP-A has been determined. PAPP-A is a monomer in solution. It has two domains: an N-terminal domain and a C-terminal domain. The N-terminal domain contains the PAPP-A active site. The C-terminal domain is responsible for binding to IGFBP substrates. PAPP-A cleaves IGFBPs at the Arg-Phe bond. The 3D structure of PAPP-A reveals that it is a enzyme.
The tertiary structure of PAPP-A is a monomer in solution. It contains two domains: an N-terminal domain and a C-terminal domain. The N-terminal domain contains the PAPP-A active site. The C-terminal domain is responsible for binding to IGFBP substrates. PAPP-A cleaves IGFBPs at the Arg-Phe bond. The 3D structure of PAPP-A reveals that it is a enzyme.
PAPP-A is a protease that is essential for the development of cardiovascular and skeletal systems. It is also involved in the turnover of extracellular matrix during embryogenesis and wound healing. PAPP-A is a metalloproteinase that cleaves insulin-like growth factor binding proteins (IGFBP) and progresses the linear IGF1 to its mature form. The protease is a type I transmembrane protein composed of 744 amino acids with a large extracellular domain, a single-pass transmembrane region, and a small cytoplasmic tail.
The three-dimensional structure of PAPP-A has been determined, and it provides insights into the metalloproteinase activity and membrane binding of this protease. PAPP-A consists of two structurally distinct regions: an N-terminal domain (residues 1-496) that is homologous to other zinc metalloproteinases, and a C-terminal domain (residues 497-744) that is unique to PAPP-A. The zinc ion is coordinated by three histidine residues in the N-terminal domain, and theactive site is located at the junction between the two domains.
The C-terminal domain contains a helix-loop-helix motif that is involved in the binding of PAPP-A to membrane substrates. This domain also mediates the higher-order oligomerization of PAPP-A, which is required for the protease activity. PAPP-A exists as a monomer in solution, but it oligomerizes to form a doughnut-shaped complex on the cell surface. This complex is composed of four monomers, and each monomer has one zinc ion coordinated by three histidine residues.
The three-dimensional structure of PAPP-A provides insights into the metalloproteinase activity and membrane binding of this protease. The protease is a type I transmembrane protein composed of 744 amino acids with a large extracellular domain, a single-pass transmembrane region, and a small cytoplasmic tail. PAPP-A consists of two structurally distinct regions: an N-terminal domain (residues 1-496) that is homologous to other zinc metalloproteinases, and a C-terminal domain (residues 497-744) that is unique to PAPP-A. The zinc ion is coordinated by three histidine residues in the N-terminal domain, and theactive site is located at the junction between the two domains.
The C-terminal domain contains a helix-loop-helix motif that is involved in the binding of PAPP-A to membrane substrates. This domain also mediates the higher-order oligomerization of PAPP-A, which is required for the protease activity. PAPP-A exists as a monomer in solution, but it oligomerizes to form a doughnut-shaped complex on the cell surface. This complex is composed of four monomers, and each monomer has one zinc ion coordinated by three histidine residues.
The three-dimensional structure of PAPP-A provides insights into how this protease cleaves IGFBP and how it is involved in the turnover of extracellular matrix during embryogenesis and wound healing.
