Epiregulin

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

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

Structure[edit]

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[edit]

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[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000124882 - Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: epiregulin".
  7. ^ a b c d 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.

Further reading[edit]

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