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| | ==Crystal structure of the GAIN and HormR domains of brain angiogenesis inhibitor 3 (BAI3)== | | ==Crystal structure of the GAIN and HormR domains of brain angiogenesis inhibitor 3 (BAI3)== |
| - | <StructureSection load='4dlo' size='340' side='right' caption='[[4dlo]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='4dlo' size='340' side='right'caption='[[4dlo]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dlo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DLO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DLO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dlo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DLO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dlq|4dlq]]</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=4dlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dlo OCA], [https://pdbe.org/4dlo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dlo RCSB], [https://www.ebi.ac.uk/pdbsum/4dlo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dlo ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAI3, KIAA0550 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dlo OCA], [http://pdbe.org/4dlo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dlo RCSB], [http://www.ebi.ac.uk/pdbsum/4dlo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dlo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BAI3_HUMAN BAI3_HUMAN]] May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. Might be involved in angiogenesis inhibition and suppression of glioblastoma. | + | [[https://www.uniprot.org/uniprot/AGRB3_HUMAN AGRB3_HUMAN]] |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Arac, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Bolliger, M F]] | + | [[Category: Arac D]] |
| - | [[Category: Boucard, A A]] | + | [[Category: Bolliger MF]] |
| - | [[Category: Brunger, A T]] | + | [[Category: Boucard AA]] |
| - | [[Category: Nguyen, J]] | + | [[Category: Brunger AT]] |
| - | [[Category: Soltis, M]] | + | [[Category: Nguyen J]] |
| - | [[Category: Sudhof, T C]] | + | [[Category: Soltis M]] |
| - | [[Category: Autoproteolytic fold]]
| + | [[Category: Sudhof TC]] |
| - | [[Category: Extracellular]]
| + | |
| - | [[Category: Gain domain]]
| + | |
| - | [[Category: Includes gps motif]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
[AGRB3_HUMAN]
Publication Abstract from PubMed
The G protein-coupled receptor (GPCR) Proteolysis Site (GPS) of cell-adhesion GPCRs and polycystic kidney disease (PKD) proteins constitutes a highly conserved autoproteolysis sequence, but its catalytic mechanism remains unknown. Here, we show that unexpectedly the approximately 40-residue GPS motif represents an integral part of a much larger approximately 320-residue domain that we termed GPCR-Autoproteolysis INducing (GAIN) domain. Crystal structures of GAIN domains from two distantly related cell-adhesion GPCRs revealed a conserved novel fold in which the GPS motif forms five beta-strands that are tightly integrated into the overall GAIN domain. The GAIN domain is evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. Functionally, the GAIN domain is both necessary and sufficient for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyse peptide bond hydrolysis. Thus, the GAIN domain embodies a unique, evolutionarily ancient and widespread autoproteolytic fold whose function is likely relevant for GPCR signalling and for multiple human diseases.
A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis.,Arac D, Boucard AA, Bolliger MF, Nguyen J, Soltis SM, Sudhof TC, Brunger AT EMBO J. 2012 Feb 14;31(6):1364-78. doi: 10.1038/emboj.2012.26. PMID:22333914[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arac D, Boucard AA, Bolliger MF, Nguyen J, Soltis SM, Sudhof TC, Brunger AT. A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis. EMBO J. 2012 Feb 14;31(6):1364-78. doi: 10.1038/emboj.2012.26. PMID:22333914 doi:10.1038/emboj.2012.26
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