2lns: Difference between revisions
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==Solution structure of AGR2 residues 41-175== | ==Solution structure of AGR2 residues 41-175== | ||
<StructureSection load='2lns' size='340' side='right'caption='[[2lns | <StructureSection load='2lns' size='340' side='right'caption='[[2lns]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lns]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2lns]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LNS FirstGlance]. <br> | ||
</td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lns OCA], [https://pdbe.org/2lns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lns RCSB], [https://www.ebi.ac.uk/pdbsum/2lns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lns ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lns OCA], [https://pdbe.org/2lns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lns RCSB], [https://www.ebi.ac.uk/pdbsum/2lns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lns ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/AGR2_HUMAN AGR2_HUMAN] Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth.<ref>PMID:18199544</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Barraclough | [[Category: Barraclough DL]] | ||
[[Category: Barraclough | [[Category: Barraclough R]] | ||
[[Category: Clarke | [[Category: Clarke CJ]] | ||
[[Category: Lian | [[Category: Lian L]] | ||
[[Category: Patel | [[Category: Patel P]] | ||
[[Category: Rudland | [[Category: Rudland PS]] | ||
Revision as of 14:09, 15 February 2023
Solution structure of AGR2 residues 41-175Solution structure of AGR2 residues 41-175
Structural highlights
FunctionAGR2_HUMAN Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth.[1] Publication Abstract from PubMedAnterior gradient 2 (AGR2) is a normal endoplasmic reticulum protein that has two important abnormal functions, amphibian limb regeneration and human cancer metastasis promotion. These normal intracellular and abnormal extracellular roles can be attributed to the multidomain structure of AGR2. The NMR structure shows that AGR2 consists of an unstructured N-terminal region followed by a thioredoxin fold. The protein exists in monomer-dimer equilibrium with a K(d) of 8.83muM, and intermolecular salt bridges involving E60 and K64 within the folded domain serve to stabilize the dimer. The unstructured region is primarily responsible for the ability of AGR2 to promote cell adhesion while dimerization is less important for this activity. The structural data of AGR2 show a separation between potential catalytic redox activity and adhesion function within the context of metastasis and development. Metastasis-Promoting Anterior Gradient 2 Protein Has a Dimeric Thioredoxin Fold Structure and a Role in Cell Adhesion.,Patel P, Clarke C, Barraclough DL, Jowitt TA, Rudland PS, Barraclough R, Lian LY J Mol Biol. 2012 Dec 26. pii: S0022-2836(12)00942-4. doi:, 10.1016/j.jmb.2012.12.009. PMID:23274113[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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