2lnt: Difference between revisions
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==Solution structure of E60A mutant AGR2== | ==Solution structure of E60A mutant AGR2== | ||
<StructureSection load='2lnt' size='340' side='right' caption='[[2lnt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='2lnt' size='340' side='right'caption='[[2lnt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lnt]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2lnt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LNT FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lns|2lns]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2lns|2lns]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AGR2, AG2, UNQ515/PRO1030 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AGR2, AG2, UNQ515/PRO1030 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lnt OCA], [https://pdbe.org/2lnt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lnt RCSB], [https://www.ebi.ac.uk/pdbsum/2lnt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lnt 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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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Barraclough, D L]] | [[Category: Barraclough, D L]] | ||
[[Category: Barraclough, R]] | [[Category: Barraclough, R]] | ||
Revision as of 13:14, 12 May 2021
Solution structure of E60A mutant AGR2Solution structure of E60A mutant AGR2
Structural highlights
Function[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.[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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