The Structure of the Extracellular Region of Human Hepsin Reveals a Serine Protease Domain and a Novel Scavenger Receptor Cysteine-Rich (SRCR) Domain

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 Å resolution structure of the extracellular component of human hepsin. This structure includes a 255-re...

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Bibliographic Details
Published in:Structure (London) 2003-09, Vol.11 (9), p.1123-1131
Main Authors: Somoza, John R, Ho, Joseph D, Luong, Christine, Ghate, Manjiri, Sprengeler, Paul A, Mortara, Kyle, Shrader, William D, Sperandio, David, Chan, Hedy, McGrath, Mary E, Katz, Bradley A
Format: Article
Language:English
Subjects:
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
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Summary: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 Å 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.
ISSN:0969-2126
1878-4186
DOI:10.1016/S0969-2126(03)00148-5