Anterior gradient protein
From Proteopedia
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== Anterior Gradient Protein 2 == | == Anterior Gradient Protein 2 == | ||
<StructureSection load='2LNS' size='350' side='right' caption='residues 41-175 of AGR2 in dimer form (PDB entry [[2lns]])' scene='87/872187/Agr2_full/1'> | <StructureSection load='2LNS' size='350' side='right' caption='residues 41-175 of AGR2 in dimer form (PDB entry [[2lns]])' scene='87/872187/Agr2_full/1'> | ||
| + | __TOC__ | ||
| + | ==Function== | ||
[https://www.uniprot.org/uniprot/AGR2_HUMAN AGR2_HUMAN] | [https://www.uniprot.org/uniprot/AGR2_HUMAN AGR2_HUMAN] | ||
Originally discovered in Xenopus laevis as a cement gland differentiation regulator <ref>PMID: 31644305</ref>, <scene name='87/872187/Agr2_full/1'>Anterior Gradient Protein 2</scene> (AGR2) in humans is a protein chaperone ([[chaperones]]) involved in '''proteostasis''', mainly for proteins expressed in epithelial cells, such as in the esophagus or lungs<ref>PMID:33005802</ref>. AGR2, composed of 175 amino acids, belongs to the protein disulfide isomerase family ([https://www.uniprot.org/uniprot/P07237 PDI]). | Originally discovered in Xenopus laevis as a cement gland differentiation regulator <ref>PMID: 31644305</ref>, <scene name='87/872187/Agr2_full/1'>Anterior Gradient Protein 2</scene> (AGR2) in humans is a protein chaperone ([[chaperones]]) involved in '''proteostasis''', mainly for proteins expressed in epithelial cells, such as in the esophagus or lungs<ref>PMID:33005802</ref>. AGR2, composed of 175 amino acids, belongs to the protein disulfide isomerase family ([https://www.uniprot.org/uniprot/P07237 PDI]). | ||
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The AGR2 protein can form complexes with [https://www.uniprot.org/uniprot/Q9Y230 Reptin] ([[2cqa]]) which is recognized as an '''anti-oncogene'''. However, it binds more easily when the protein is in dimeric form. Thus, a mutation on (<scene name='87/872187/Agr2_e60/2'>E60</scene>) site, giving the protein a monomeric form, would reduce cancer repression by Reptin. | The AGR2 protein can form complexes with [https://www.uniprot.org/uniprot/Q9Y230 Reptin] ([[2cqa]]) which is recognized as an '''anti-oncogene'''. However, it binds more easily when the protein is in dimeric form. Thus, a mutation on (<scene name='87/872187/Agr2_e60/2'>E60</scene>) site, giving the protein a monomeric form, would reduce cancer repression by Reptin. | ||
Finally, the expression of AGR2 in breast cancer patients confers chemoresistance to cancer cell growth inhibitors such as Tamoxifen, the mechanism is still unclear.<ref>PMID: 25937245</ref> | Finally, the expression of AGR2 in breast cancer patients confers chemoresistance to cancer cell growth inhibitors such as Tamoxifen, the mechanism is still unclear.<ref>PMID: 25937245</ref> | ||
| - | </StructureSection> | ||
== 3D Structures of anterior gradient protein == | == 3D Structures of anterior gradient protein == | ||
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== References == | == References == | ||
<references/> | <references/> | ||
| + | </StructureSection> | ||
| + | [[Category:Topic Page]] | ||
Current revision
Anterior Gradient Protein 2
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Proteopedia Page Contributors and Editors (what is this?)
Loane Schertzer, Michal Harel, Marion Ottinger, Léa Moyon, Jaime Prilusky
