Structure of HBP, a multifunctional protein with a serine proteinase fold.
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.
Iversen
L F
LF
Kastrup
J S
JS
Bjørn
S E
SE
Rasmussen
P B
PB
Wiberg
F C
FC
Flodgaard
H J
HJ
Larsen
I K
IK
D023181:Antimicrobial Cationic Peptides; D001665:Binding Sites; D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism; D002352:Carrier Proteins; D003198:Computer Simulation; D004731:Endotoxins / Q000378:metabolism; D006493:Heparin / Q000378:metabolism; D006801:Humans; D019272:Leukocyte Elastase / Q000737:chemistry; D008050:Lipid A / Q000378:metabolism; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism
C062991:AZU1 protein, human; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D002352:Carrier Proteins; D004731:Endotoxins; D008050:Lipid A; D006493:Heparin; D012697:Serine Endopeptidases; D019272:Leukocyte Elastase