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Anterior gradient protein: Difference between revisions

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== Anterior Gradient Protein 2 ==
== Anterior Gradient Protein 2 ==
Originally discovered in Xenopus laevis as a cement gland differentiation regulator, <scene name='87/872187/Agr2_structure/2'>Anterior Gradient Protein</scene> (AGR2) in humans is a protein chaperone involved in proteostasis, mainly for proteins expressed in epithelial cells, such as in the esophagus or lungs. AGR2, composed of 175 amino acids, belongs to the protein disulfide isomerase family (PDI).  
Originally discovered in Xenopus laevis as a cement gland differentiation regulator, <scene name='87/872187/Agr2_structure/2'>Anterior Gradient Protein</scene> (AGR2) in humans is a protein chaperone involved in proteostasis, mainly for proteins expressed in epithelial cells, such as in the esophagus or lungs. AGR2, composed of 175 amino acids, belongs to the protein disulfide isomerase family (PDI).  


== Structural highlights ==
== Structural highlights ==
<StructureSection load='2LNS' size='350' side='right' caption='Escherichia coli reca protein-bound DNA (PDB entry [[3rec]])' scene=''>


<Structure load='2LNS' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
This protein contains various remarkable domains which can be visualized in the figure.


This protein contains various remarkable domains which can be visualized in the figure.
an unfolded NH2 terminal sequence with a peptide signal from the first to the 21st amino acid  
- an unfolded NH2 terminal sequence with a peptide signal from the first to the 21st amino acid  
- an active pseudo-thioredoxin domain (CXXS) from the 81st to the 84th amino acid. Called “pseudo” because there is only one active cysteine residue (C81).
- an active <scene name='87/872187/Agr2_cxxs/1'>pseudo-thioredoxin domain</scene> (CXXS) from the 81st to the 84th amino acid. Called “pseudo” because there is only one active <scene name='87/872187/Agr2_c81/1'>cysteine residue</scene> (C81).
- a terminal COOH sequence with a KTEL motif from the 172nd to the last   
- a terminal COOH sequence with a KTEL motif from the 172nd to the last   
Moreover, this protein can be found as a monomer or a dimer, thanks to a specific motif which is EALYK between the 60th and the 64th amino acids. There are intermolecular salt bridges involving E60 and K64, in order to fix the second monomer. The CXXS domain is on the opposite side to avoid any disulfide exchange. Nevertheless, the dimeric structure is oxidation-dependent which means that C81 is necessary.  
Moreover, this protein can be found as a monomer or a dimer, thanks to a specific motif which is EALYK between the 60th and the 64th amino acids. There are intermolecular salt bridges involving E60 and K64, in order to fix the second monomer. The CXXS domain is on the opposite side to avoid any disulfide exchange. Nevertheless, the dimeric structure is oxidation-dependent which means that C81 is necessary.  
</StructureSection>




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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.




== References ==
== References ==
<references/>
<references/>

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Loane Schertzer, Marion Ottinger, Léa Moyon, Michal Harel, Jaime Prilusky
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