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PRG2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1H8U, 2BRS, 4QXX
Identifiers
Aliases	PRG2, BMPG, MBP, MBP1, proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein), proMBP, proteoglycan 2, pro eosinophil major basic protein
External IDs	OMIM: 605601; MGI: 103294; HomoloGene: 2044; GeneCards: PRG2; OMA:PRG2 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	57,390,650 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	84,813,976 bp
RNA expression pattern
	Top expressed in
	placenta; ; bone marrow; ; bone marrow cells; ; right lobe of liver; ; skin of leg; ; subcutaneous adipose tissue; ; spleen; ; skin of abdomen; ; monocyte; ; blood;
	Top expressed in
	tibiofemoral joint; ; granulocyte; ; fetal liver hematopoietic progenitor cell; ; bone marrow; ; embryo; ; embryo; ; ankle joint; ; spleen; ; human fetus; ; vestibular membrane of cochlear duct;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	heparin binding; carbohydrate binding; extracellular matrix structural constituent conferring compression resistance;
Cellular component	extracellular region; transport vesicle; cytoplasmic vesicle; extracellular exosome; ficolin-1-rich granule lumen; collagen-containing extracellular matrix;
Biological process	defense response to bacterium; immune system process; defense response to nematode; negative regulation of interleukin-10 production; positive regulation of interleukin-4 production; immune response; neutrophil degranulation;
	Sources:Amigo / QuickGO
Orthologs
	5553
	19074
	ENSG00000186652
	ENSMUSG00000027073
	P13727
	Q61878
	NM_002728; NM_001243245; NM_001302926; NM_001302927
	NM_008920
	NP_001230174; NP_001289855; NP_001289856; NP_002719
	NP_032946
	Wikidata
View/Edit Human	View/Edit Mouse

Eosinophil major basic protein, often shortened to major basic protein (MBP; also called proteoglycan 2 (PRG2)) is encoded in humans by the PRG2 gene.^[5]

Function

The protein encoded by this gene is the predominant constituent of the crystalline core of the eosinophil granule. High levels of the proform of this protein are also present in placenta and pregnancy serum, where it exists as a complex with several other proteins including pregnancy-associated plasma protein A (PAPPA), angiotensinogen (AGT), and C3dg. This protein may be involved in antiparasitic defense mechanisms as a cytotoxin and helmintho-toxin, and in immune hypersensitivity reactions. It is directly implicated in epithelial cell damage, exfoliation, and bronchospasm in allergic diseases.^[5]

PRG2 is a 117-residue protein that predominates in eosinophil granules. It is a potent enzyme against helminths and is toxic towards bacteria and mammalian cells in vitro. The eosinophil major basic protein also causes the release of histamine from mast cells and basophils, and activates neutrophils and alveolar macrophages.

Structure

Structurally the major basic protein (MBP) is similar to lectins (sugar-binding proteins), and has a fold similar to that seen in C-type lectins. However, unlike other C-type lectins (those that bind various carbohydrates in the presence of calcium), MBP does not bind either calcium or any of the other carbohydrates that this family recognize.

Instead, MBP recognises heparan sulfate proteoglycans. Two crystallographic structures of MBP have been determined.^[6]^[7]

Interactions

Major basic protein has been shown to interact with pregnancy-associated plasma protein A.^[8]^[9]^[10]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000186652 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000027073 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: PRG2 proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein)".
^ PDB: 1h8u; Swaminathan GJ, Weaver AJ, Loegering DA, Checkel JL, Leonidas DD, Gleich GJ, Acharya KR (July 2001). "Crystal structure of the eosinophil major basic protein at 1.8 A. An atypical lectin with a paradigm shift in specificity". J. Biol. Chem. 276 (28): 26197–26203. doi:10.1074/jbc.M100848200. PMID 11319227.
^ PDB: 2brs; Swaminathan GJ, Myszka DG, Katsamba PS, Ohnuki LE, Gleich GJ, Acharya KR (November 2005). "Eosinophil-granule major basic protein, a C-type lectin, binds heparin". Biochemistry. 44 (43): 14152–14158. doi:10.1021/bi051112b. PMID 16245931.
^ Overgaard MT, Haaning J, Boldt H B, Olsen I M, Laursen L S, Christiansen M, Gleich G J, Sottrup-Jensen L, Conover C A, Oxvig C (October 2000). "Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor". J. Biol. Chem. 275 (40). UNITED STATES: 31128–31133. doi:10.1074/jbc.M001384200. ISSN 0021-9258. PMID 10913121.
^ Overgaard MT, Sorensen ES, Stachowiak D, Boldt HB, Kristensen L, Sottrup-Jensen L, Oxvig C (January 2003). "Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachment". J. Biol. Chem. 278 (4). United States: 2106–2117. doi:10.1074/jbc.M208777200. ISSN 0021-9258. PMID 12421832.
^ Oxvig C, Sand O, Kristensen T, Gleich G J, Sottrup-Jensen L (June 1993). "Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein". J. Biol. Chem. 268 (17). UNITED STATES: 12243–6. doi:10.1016/S0021-9258(18)31378-4. ISSN 0021-9258. PMID 7685339.

External links

Eosinophil+Major+Basic+Protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Overview of all the structural information available in the PDB for UniProt: P13727 (Bone marrow proteoglycan) at the PDBe-KB.