Structure of HBP, a multifunctional protein with a serine proteinase fold

Nat Struct Biol. 1997 Apr;4(4):265-8. doi: 10.1038/nsb0497-265.

Abstract

The structure of human heparin binding protein reveals that the serine proteinase fold has been used as a scaffold for a multifunctional protein with antibacterial activity, monocyte and t-cell activating properties and endotoxin and heparin binding capacity.

Publication types

  • Comparative Study
  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antimicrobial Cationic Peptides
  • Binding Sites
  • Blood Proteins / chemistry*
  • Blood Proteins / metabolism
  • Carrier Proteins*
  • Computer Simulation
  • Endotoxins / metabolism
  • Heparin / metabolism
  • Humans
  • Leukocyte Elastase / chemistry
  • Lipid A / metabolism
  • Models, Molecular
  • Protein Structure, Tertiary*
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / metabolism

Substances

  • Antimicrobial Cationic Peptides
  • Blood Proteins
  • Carrier Proteins
  • Endotoxins
  • Lipid A
  • cationic antimicrobial protein CAP 37, human
  • Heparin
  • Serine Endopeptidases
  • Leukocyte Elastase