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PGLYRP1  -  peptidoglycan recognition protein 1

Bos taurus

 
 
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Disease relevance of PGLYRP

  • The herpes simplex virus type 1 origin of DNA replication, oriS, contains three copies of the recognition sequence for the viral initiator protein, origin binding protein (OBP), arranged in two palindromes [1].
  • We have used intact OBP as well as a truncated form of the protein expressed in Escherichia coli to investigate the protein-protein interactions, as well as the protein-DNA interactions involved in the formation of a nucleoprotein complex at a viral origin of replication (oriS) in vitro [2].
  • These results suggest that OBP, which is expressed at millimolar levels, might reduce HNE toxicity by removing from the nasal mucus a significant fraction of the aldehyde that is produced as a consequence of direct exposure to the oxygen present in inhaled air [3].
 

Psychiatry related information on PGLYRP

  • In light of these findings, and published results for other mammalian OBP-ligand complexes, a general model for the role of OBPs in mammalian olfaction is proposed [4].
 

High impact information on PGLYRP

 

Biological context of PGLYRP

  • The origin binding protein (OBP) of herpes simplex virus type 1 is required to activate a viral origin of replication in vivo [2].
  • This suggests that OBP is unlikely to play a role only in olfactory signal transduction [8].
  • The binding was selective for mu-agonists, stereospecific and inhibited by GTP gamma S. These results demonstrate that there is recoupling of OBP with G-protein and confirm our earlier evidence that the purified OBP is a mu-opioid binding site [9].
  • The partial amino acid sequences of the three OBPs, determined by Edman degradation, confirm that they are members of the OBP family, but reveal poor similarity between them [10].
  • This study investigated the binding properties and chemical resistance of OBP to the chemically reactive lipid peroxidation end-product 4-hydroxy-2-nonenal (HNE), in an attempt to establish a functional relationship between this protein and the molecular mechanisms combating free radical cellular damage [3].
 

Anatomical context of PGLYRP

 

Associations of PGLYRP with chemical compounds

  • The existence of domains in the OBP, which are antigenically similar to those in two other guanine nucleotide regulatory protein-coupled receptors, supports the hypothesis that mu opioid receptors have the structure characteristic of this receptor family [7].
  • Although OBP was originally isolated as a pyrazine binding protein, both rat and bovine OBP also bind the odorants [3H]methyldihydrojasmonate and 3,7-dimethyl-octan-1-ol as well as 2-isobutyl-3-[3H]methoxypyrazine [12].
  • With the exception of rat and mouse major urinary proteins, which exhibit a high degree of structural similarity with OBP and bind similar ligands, other members of the lipocalin family, such as retinol-binding protein and beta-lactoglobulin, failed to inhibit the binding of 125I-labelled OBP to its receptor [8].
  • Furthermore, OBP functionality, as determined by measuring the binding of the fluorescent ligand 1-aminoanthracene, was partially lost only when incubating HNE levels and exposure time to HNE exceeded physiological values in nasal mucosa [3].
 

Analytical, diagnostic and therapeutic context of PGLYRP

References

  1. Complementary intrastrand base pairing during initiation of Herpes simplex virus type 1 DNA replication. Aslani, A., Macao, B., Simonsson, S., Elias, P. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  2. Structural elements required for the cooperative binding of the herpes simplex virus origin binding protein to oriS reside in the N-terminal part of the protein. Elias, P., Gustafsson, C.M., Hammarsten, O., Stow, N.D. J. Biol. Chem. (1992) [Pubmed]
  3. Odorant binding protein has the biochemical properties of a scavenger for 4-hydroxy-2-nonenal in mammalian nasal mucosa. Grolli, S., Merli, E., Conti, V., Scaltriti, E., Ramoni, R. FEBS J. (2006) [Pubmed]
  4. Molecular and functional characterization of an odorant binding protein of the Asian elephant, Elephas maximus: implications for the role of lipocalins in mammalian olfaction. Lazar, J., Greenwood, D.R., Rasmussen, L.E., Prestwich, G.D. Biochemistry (2002) [Pubmed]
  5. The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition. Bianchet, M.A., Bains, G., Pelosi, P., Pevsner, J., Snyder, S.H., Monaco, H.L., Amzel, L.M. Nat. Struct. Biol. (1996) [Pubmed]
  6. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Tegoni, M., Ramoni, R., Bignetti, E., Spinelli, S., Cambillau, C. Nat. Struct. Biol. (1996) [Pubmed]
  7. Immunoblots with rhodopsin antisera suggest that a purified mu opioid binding protein has structural characteristics of a G-protein-coupled receptor. Gioannini, T.L., Weiss, E.R., Johnson, G.L., Hiller, J.M., Simon, E.J. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  8. Membrane receptor for odour-binding proteins. Boudjelal, M., Sivaprasadarao, A., Findlay, J.B. Biochem. J. (1996) [Pubmed]
  9. Reconstitution of a purified mu-opioid binding protein in liposomes: selective, high affinity, GTP gamma S-sensitive mu-opioid agonist binding is restored. Gioannini, T.L., Fan, L.Q., Hyde, L., Ofri, D., Yao, Y.H., Hiller, J.M., Simon, E.J. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  10. Three odorant-binding proteins from rabbit nasal mucosa. Garibotti, M., Navarrini, A., Pisanelli, A.M., Pelosi, P. Chem. Senses (1997) [Pubmed]
  11. Isolation, characterization, and antimicrobial properties of bovine oligosaccharide-binding protein. A microbicidal granule protein of eosinophils and neutrophils. Tydell, C.C., Yount, N., Tran, D., Yuan, J., Selsted, M.E. J. Biol. Chem. (2002) [Pubmed]
  12. Odorant-binding protein: localization to nasal glands and secretions. Pevsner, J., Sklar, P.B., Snyder, S.H. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  13. Bovine peptidoglycan recognition protein-S: antimicrobial activity, localization, secretion, and binding properties. Tydell, C.C., Yuan, J., Tran, P., Selsted, M.E. J. Immunol. (2006) [Pubmed]
 
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