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3  structures 110  species 1  interaction 774  sequences 9  architectures

Family: LBP_BPI_CETP (PF01273)

Summary: LBP / BPI / CETP family, N-terminal domain

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This is the Wikipedia entry entitled "Lipid-binding serum glycoprotein". More...

Lipid-binding serum glycoprotein Edit Wikipedia article

LBP / BPI / CETP family, N-terminal domain
PDB 1bp1 EBI.jpg
crystal structure of bpi, the human bactericidal permeability-increasing protein
Identifiers
Symbol LBP_BPI_CETP
Pfam PF01273
InterPro IPR017942
PROSITE PDOC00367
SCOP 1bp1
SUPERFAMILY 1bp1
TCDB 1.C.40
OPM superfamily 452
OPM protein 2obd
LBP / BPI / CETP family, C-terminal domain
PDB 1bp1 EBI.jpg
crystal structure of bpi, the human bactericidal permeability-increasing protein
Identifiers
Symbol LBP_BPI_CETP_C
Pfam PF02886
InterPro IPR001124
PROSITE PDOC00367
SCOP 1bp1
SUPERFAMILY 1bp1
TCDB 1.C.40

In molecular biology, the lipid-binding serum glycoproteins family, also known as the BPI/LBP/Plunc family or LBP/BPI/CETP family represents a family which includes mammalian lipid-binding serum glycoproteins. Members of this family include:

These proteins consist of N- and C-terminal domains, which share a similar two-layer alpha/beta structure, but show little sequence identity to each other.

Bactericidal permeability-increasing protein (BPI) is a potent antimicrobial protein of 456 amino acids that binds to and neutralises lipopolysaccharides from the outer membrane of Gram-negative bacteria.[4] BPI contains two domains that adopt the same structural fold, even though they have little sequence similarity.[5]

Lipopolysaccharide-binding protein (LBP) is an endotoxin-binding protein that is closely related to, and functions in a co-ordinated manner with BPI to facilitate an integrated host response to invading Gram-negative bacteria.[6]

Cholesteryl ester transfer protein (CETP) is a glycoprotein that facilitates the transfer of lipids (cholesteryl esters and triglycerides) between the different lipoproteins that transport them through plasma, including HDL, LDL, VLDL and chylomicrons. These lipoproteins shield the lipids from water by encapsulating them within a coating of polar lipids and proteins.[7]

Phospholipid transfer protein (PLTP) exchanges phospholipids between lipoproteins and remodels high-density lipoproteins (HDLs).[8]

Palate, lung and nasal epithelium carcinoma-associated protein (PLUNC) is a potential host defensive protein that is secreted from the submucosal gland to the saliva and nasal lavage fluid. PLUNC appears to be a secreted product of neutrophil granules that participates in an aspect of the inflammatory response that contributes to host defence.[9] Short palate, lung and nasal epithelium clone 1 (SPLUNC1) may bind the lipopolysaccharide of Gram-negative nanobacteria, thereby playing an important role in the host defence of nasopharyngeal epithelium.[10]

Human proteins belonging to this family[edit]

BPI; BPIL1; BPIL2; BPIL3; CETP; LBP; LPLUNC1; LPLUNC3; LPLUNC4; PLTP; PLUNC; SPLUNC2;

References[edit]

  1. ^ Gray PW, Flaggs G, Leong SR, Gumina RJ, Weiss J, Ooi CE, Elsbach P (1989). "Cloning of the cDNA of a human neutrophil bactericidal protein. Structural and functional correlations". J. Biol. Chem. 264 (16): 9505–9509. PMID 2722846. 
  2. ^ Gray PW, Leong SR, Wright SD, Schumann RR, Flaggs GW, Mathison JC, Tobias PS, Ulevitch RJ (1990). "Structure and function of lipopolysaccharide binding protein". Science 249 (4975): 1429–1431. doi:10.1126/science.2402637. PMID 2402637. 
  3. ^ Grant FJ, Day JR, Albers JJ, Lofton-Day CE, Gilbert TL, Marcovina SM, Adolphson JL, O Hara PJ, Ching AF (1994). "Complete cDNA encoding human phospholipid transfer protein from human endothelial cells". J. Biol. Chem. 269 (12): 9388–9391. PMID 8132678. 
  4. ^ Beamer LJ, Carroll SF, Eisenberg D (June 1997). "Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution". Science 276 (5320): 1861–4. doi:10.1126/science.276.5320.1861. PMID 9188532. 
  5. ^ Kleiger G, Beamer LJ, Grothe R, Mallick P, Eisenberg D (June 2000). "The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold". J. Mol. Biol. 299 (4): 1019–34. doi:10.1006/jmbi.2000.3805. PMID 10843855. 
  6. ^ Weiss J (August 2003). "Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): structure, function and regulation in host defence against Gram-negative bacteria". Biochem. Soc. Trans. 31 (Pt 4): 785–90. PMID 12887306. 
  7. ^ Hamilton JA, Deckelbaum RJ (February 2007). "Crystal structure of CETP: new hopes for raising HDL to decrease risk of cardiovascular disease?". Nat. Struct. Mol. Biol. 14 (2): 95–7. doi:10.1038/nsmb0207-95. PMID 17277799. 
  8. ^ Ponsin G, Qu SJ, Fan HZ, Pownall HJ (April 2003). "Structural and functional determinants of human plasma phospholipid transfer protein activity as revealed by site-directed mutagenesis of charged amino acids". Biochemistry 42 (15): 4444–51. doi:10.1021/bi027006g. PMID 12693940. 
  9. ^ Bartlett JA, Hicks BJ, Schlomann JM, Ramachandran S, Nauseef WM, McCray PB (May 2008). "PLUNC is a secreted product of neutrophil granules". J. Leukoc. Biol. 83 (5): 1201–6. doi:10.1189/jlb.0507302. PMID 18245229. 
  10. ^ Zhou HD, Li GY, Yang YX, Li XL, Sheng SR, Zhang WL, Zhao J (April 2006). "Intracellular co-localization of SPLUNC1 protein with nanobacteria in nasopharyngeal carcinoma epithelia HNE1 cells depended on the bactericidal permeability increasing protein domain". Mol. Immunol. 43 (11): 1864–71. doi:10.1016/j.molimm.2005.10.021. PMID 16364440. 

This article incorporates text from the public domain Pfam and InterPro IPR017942

This article incorporates text from the public domain Pfam and InterPro IPR001124

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

LBP / BPI / CETP family, N-terminal domain Provide feedback

The N and C terminal domains of the LBP/BPI/CETP family are structurally similar.

Literature references

  1. Beamer LJ, Carroll SF, Eisenberg D; , Science 1997;276:1861-1864.: Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. PUBMED:9188532 EPMC:9188532


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR017942

This entry represents the N-terminal domain found in several lipid-binding serum glycoproteins. The N- and C-terminal domains share a similar two-layer alpha/beta structure, but they show little sequence identity. Proteins containing this N-terminal domain include:

  • Bactericidal permeability-increasing protein (BPI)
  • Lipopolysaccharide-binding protein (LBP)
  • Cholesteryl ester transfer protein (CETP)
  • Phospholipid transfer protein (PLTP)
  • Palate, lung and nasal epithelium carcinoma-associated protein (PLUNC)

Bactericidal permeability-increasing protein (BPI) is a potent antimicrobial protein of 456 residues that binds to and neutralises lipopolysaccharides from the outer membrane of Gram-negative bacteria [PUBMED:9188532]. BPI contains two domains that adopt the same structural fold, even though they have little sequence similarity [PUBMED:10843855].

Lipopolysaccharide-binding protein (LBP) is an endotoxin-binding protein that is closely related to, and functions in a co-ordinated manner with BPI to facilitate an integrated host response to invading Gram-negative bacteria [PUBMED:12887306].

Cholesteryl ester transfer protein (CETP) is a glycoprotein that facilitates the transfer of lipids (cholesteryl esters and triglycerides) between the different lipoproteins that transport them through plasma, including HDL, LDL, VLDL and chylomicrons. These lipoproteins shield the lipids from water by encapsulating them within a coating of polar lipids and proteins [PUBMED:17277799].

Phospholipid transfer protein (PLTP) exchanges phospholipids between lipoproteins and remodels high-density lipoproteins (HDLs) [PUBMED:12693940].

Palate, lung and nasal epithelium carcinoma-associated protein (PLUNC) is a potential host defensive protein that is secreted from the submucosal gland to the saliva and nasal lavage fluid. PLUNC appears to be a secreted product of neutrophil granules that participates in an aspect of the inflammatory response that contributes to host defence [PUBMED:18245229]. Short palate, lung and nasal epithelium clone 1 (SPLUNC1) may bind the lipopolysaccharide of Gram-negative nanobacteria, thereby playing an important role in the host defence of nasopharyngeal epithelium [PUBMED:16364440].

Gene Ontology

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Domain organisation

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Alignments

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(36)
Full
(774)
Representative proteomes NCBI
(720)
Meta
(0)
RP15
(64)
RP35
(88)
RP55
(182)
RP75
(412)
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  Seed
(36)
Full
(774)
Representative proteomes NCBI
(720)
Meta
(0)
RP15
(64)
RP35
(88)
RP55
(182)
RP75
(412)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: Lipid_binding_gp;
Type: Family
Author: Finn RD, Bateman A, Griffiths-Jones SR
Number in seed: 36
Number in full: 774
Average length of the domain: 166.10 aa
Average identity of full alignment: 17 %
Average coverage of the sequence by the domain: 38.69 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 28.3 28.3
Trusted cut-off 28.8 28.3
Noise cut-off 28.1 28.0
Model length: 164
Family (HMM) version: 20
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Interactions

There is 1 interaction for this family. More...

LBP_BPI_CETP_C

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the LBP_BPI_CETP domain has been found. There are 3 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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