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Gene Review

PGLYRP3  -  peptidoglycan recognition protein 3

Homo sapiens

Synonyms: PGLYRPIalpha, PGRP-I-alpha, PGRP-Ialpha, PGRPIA, Peptidoglycan recognition protein 3, ...
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Disease relevance of PGLYRP3


High impact information on PGLYRP3

  • We determined the crystal structure, at 2.30-A resolution, of the C-terminal PGN-binding domain of human PGRP-Ialpha in complex with a muramyl tripeptide representing the core of lysine-type PGNs from Gram-positive bacteria [3].
  • PGLYRP3 and PGLYRP4 are also active in vivo and protect mice against experimental lung infection [1].
  • Furthermore, the compounds that contained only a stem peptide (pentapeptide, compound 1) and (DAP-PP, compound 2) as well as muramyldipeptide (compound 3) exhibited no binding indicating that the muramyltripeptide (compound 4) is the smallest peptidoglycan fragment that can be recognized by PGRP-Ialpha [4].
  • Dimerization of PGRP-Ialpha, which occurs through three-dimensional domain swapping, is mediated by specific binding of sodium ions to a flexible hinge loop, stabilizing the conformation found in the dimer [5].
  • These synthetic PAMPs markedly upregulated the mRNA expression of the four PGRPs and cell surface expression of PGRP-Ialpha and -Ibeta, but did not induce either mRNA expression or secretion of inflammatory cytokines, in oral epithelial cells [6].

Chemical compound and disease context of PGLYRP3


Biological context of PGLYRP3


Anatomical context of PGLYRP3


Associations of PGLYRP3 with chemical compounds

  • The structure reveals important features not observed previously in the complex between PGRP-Ialpha and a muramyl tripeptide lacking D-Ala at stem positions 4 and 5 [7].
  • The binding profiles were rationalized by using a recently reported x-ray crystal structure of PGRP-Ialpha with the lysine-containing muramyltripeptide (4) [4].

Regulatory relationships of PGLYRP3

  • PGLYRP-1 is expressed primarily in the granules of polymorphonuclear leucocytes (PMNs) , and PGLYRP-3 and PGLYRP-4 are expressed in the skin, eyes, salivary glands, throat, tongue, esophagus, stomach and intestine, and protect the host against infections [9].

Analytical, diagnostic and therapeutic context of PGLYRP3


  1. Peptidoglycan recognition proteins are a new class of human bactericidal proteins. Lu, X., Wang, M., Qi, J., Wang, H., Li, X., Gupta, D., Dziarski, R. J. Biol. Chem. (2006) [Pubmed]
  2. Peptidoglycan recognition proteins Pglyrp3 and Pglyrp4 are encoded from the epidermal differentiation complex and are candidate genes for the Psors4 locus on chromosome 1q21. Sun, C., Mathur, P., Dupuis, J., Tizard, R., Ticho, B., Crowell, T., Gardner, H., Bowcock, A.M., Carulli, J. Hum. Genet. (2006) [Pubmed]
  3. Structural basis for peptidoglycan binding by peptidoglycan recognition proteins. Guan, R., Roychowdhury, A., Ember, B., Kumar, S., Boons, G.J., Mariuzza, R.A. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  4. Selective recognition of synthetic lysine and meso-diaminopimelic acid-type peptidoglycan fragments by human peptidoglycan recognition proteins I{alpha} and S. Kumar, S., Roychowdhury, A., Ember, B., Wang, Q., Guan, R., Mariuzza, R.A., Boons, G.J. J. Biol. Chem. (2005) [Pubmed]
  5. Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ialpha. Guan, R., Malchiodi, E.L., Wang, Q., Schuck, P., Mariuzza, R.A. J. Biol. Chem. (2004) [Pubmed]
  6. Chemically synthesized pathogen-associated molecular patterns increase the expression of peptidoglycan recognition proteins via toll-like receptors, NOD1 and NOD2 in human oral epithelial cells. Uehara, A., Sugawara, Y., Kurata, S., Fujimoto, Y., Fukase, K., Kusumoto, S., Satta, Y., Sasano, T., Sugawara, S., Takada, H. Cell. Microbiol. (2005) [Pubmed]
  7. Crystal structure of human peptidoglycan recognition protein I{alpha} bound to a muramyl pentapeptide from Gram-positive bacteria. Guan, R., Brown, P.H., Swaminathan, C.P., Roychowdhury, A., Boons, G.J., Mariuzza, R.A. Protein Sci. (2006) [Pubmed]
  8. Peptidoglycan recognition proteins: a novel family of four human innate immunity pattern recognition molecules. Liu, C., Xu, Z., Gupta, D., Dziarski, R. J. Biol. Chem. (2001) [Pubmed]
  9. Mammalian PGRPs: novel antibacterial proteins. Dziarski, R., Gupta, D. Cell. Microbiol. (2006) [Pubmed]
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