Bacteria permeabilizing protein
| Bacteria permeabilizing protein | ||
|---|---|---|
|
||
| Ribbon model from the side, according to PDB 1EWF | ||
| Properties of human protein | ||
| Mass / length primary structure | 456 amino acids | |
| Secondary to quaternary structure | Monomer, dimer | |
| Precursor | (487 aa) | |
| Identifier | ||
| Gene name | BPI | |
| External IDs | ||
| Transporter classification | ||
| TCDB | 1.C.40 | |
| designation | BPIP family | |
| Occurrence | ||
| Parent taxon | Mammals | |
The bacteria-permeabilizing protein ( BPIP , from English Bactericidal / Permeability Increasing Protein ; gene name: BPI ) is a lipid-binding and pore-forming protein in mammals . It is an important part of the innate immune response to gram-negative bacteria . In addition to its bactericidal function, BPIP makes an important contribution to the highly sensitive detection of gram-negative bacteria and, by neutralizing lipopolysaccharide , it can prevent the development of a septic shock caused by an excessive immune response. BPIP is formed and released in the granules of polymorphonuclear leukocytes .
Human BPI (huBPI) is an approx. 55 kDa glycoprotein that was originally isolated from the azurophilic granules of human neutrophils.
literature
- LJ Beamer, SF Carroll, D. Eisenberg: Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. In: Science. Volume 276, Number 5320, June 1997, pp. 1861-1864, ISSN 0036-8075 . PMID 9188532 .