Epiregulin

Epiregulin (EPR) is a protein that in humans is encoded by the EREG gene.[5][6]

EREG
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesEREG, EPR, ER, Ep, epiregulin
External IDsOMIM: 602061 MGI: 107508 HomoloGene: 1097 GeneCards: EREG
Gene location (Human)
Chr.Chromosome 4 (human)[1]
Band4q13.3Start74,365,145 bp[1]
End74,388,749 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

2069

13874

Ensembl

ENSG00000124882

ENSMUSG00000029377

UniProt

O14944

Q61521

RefSeq (mRNA)

NM_001432

NM_007950

RefSeq (protein)

NP_001423

NP_031976

Location (UCSC)Chr 4: 74.37 – 74.39 MbChr 5: 91.07 – 91.09 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Structure

Epiregulin consists of 46 amino acid residues. Its secondary structure contains approximately 30 percent of β-sheet in the strand.[7] Some of the residues form loops and turns due to the hydrogen bonding.[7] The percentage of β-sheet in epiregulin depends on the domain and the secondary structures that they occupy. The polymeric molecules of epiregulin has the formula weight of 5280.1 g/mol with a polypeptide(L), a polymer type.[7]

Structural motifs in most proteins have typical connections in an all β motif. Meaning that the polypeptide chains do not make a crossover connection or in so far as this type of connection has not been observed. Epiregulin is one of the proteins that occupies a typical connection in all β motif. Furthermore, as the structure of epiregulin forms a chain in an all β motif, it also forms β hairpin structural motif. A β hairpin is when the two adjacent anti-parallel β strands connected by a β-turn.

Function

Epiregulin is a member of the epidermal growth factor family. Epiregulin can function as a ligand of epidermal growth factor receptor (EGFR), as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.[6] The secondary structure at the C-terminus epiregulin is different from other epidermal growth factor family ligands because of the lack of hydrogen bonds. The structural difference at the C-terminus may provide an explanation for the reduced binding affinity of epiregulin to the ERBB receptors.[7]

References

  1. GRCh38: Ensembl release 89: ENSG00000124882 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000029377 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Toyoda H, Komurasaki T, Uchida D, Morimoto S (August 1997). "Distribution of mRNA for human epiregulin, a differentially expressed member of the epidermal growth factor family". Biochem. J. 326 (1): 69–75. doi:10.1042/bj3260069. PMC 1218638. PMID 9337852.
  6. "Entrez Gene: epiregulin".
  7. Sato K, Nakamura T, Mizuguchi M, Miura K, Tada M, Aizawa T, Gomi T, Miyamoto K, Kawano K (October 2003). "Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity". FEBS Lett. 553 (3): 232–8. doi:10.1016/s0014-5793(03)01005-6. PMID 14572630. S2CID 24761378.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.