The structure of the extracellular region of human hepsin reveals a serine protease domain and a novel scavenger receptor cysteine-rich (SRCR) domain

Structure. 2003 Sep;11(9):1123-31. doi: 10.1016/s0969-2126(03)00148-5.


Hepsin is an integral membrane protein that may participate in cell growth and in maintaining proper cell morphology and is overexpressed in a number of primary tumors. We have determined the 1.75 A resolution structure of the extracellular component of human hepsin. This structure includes a 255-residue trypsin-like serine protease domain and a 109-residue region that forms a novel, poorly conserved, scavenger receptor cysteine-rich (SRCR) domain. The two domains are associated with each other through a single disulfide bond and an extensive network of noncovalent interactions. The structure suggests how the extracellular region of hepsin may be positioned with respect to the plasma membrane.

MeSH terms

  • Amino Acid Sequence
  • Cell Membrane / chemistry
  • Extracellular Space / chemistry*
  • Humans
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Receptors, Immunologic / chemistry*
  • Receptors, Scavenger
  • Sequence Alignment
  • Serine Endopeptidases / chemistry*


  • Receptors, Immunologic
  • Receptors, Scavenger
  • Serine Endopeptidases
  • hepsin

Associated data

  • PDB/1P57