1ae5
HUMAN HEPARIN BINDING PROTEINHUMAN HEPARIN BINDING PROTEIN
Structural highlights
FunctionCAP7_HUMAN This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structure of HBP, a multifunctional protein with a serine proteinase fold.,Iversen LF, Kastrup JS, Bjorn SE, Rasmussen PB, Wiberg FC, Flodgaard HJ, Larsen IK Nat Struct Biol. 1997 Apr;4(4):265-8. PMID:9095193[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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