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| | <StructureSection load='3qr2' size='340' side='right'caption='[[3qr2]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3qr2' size='340' side='right'caption='[[3qr2]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3qr2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QR2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3qr2]] 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=3QR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QR2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qqn|3qqn]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSG, UNQ6505/PRO21383 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3qr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr2 OCA], [https://pdbe.org/3qr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qr2 RCSB], [https://www.ebi.ac.uk/pdbsum/3qr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qr2 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=3qr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr2 OCA], [https://pdbe.org/3qr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qr2 RCSB], [https://www.ebi.ac.uk/pdbsum/3qr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qr2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/BASI_HUMAN BASI_HUMAN]] Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to the plasma membrane. Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes.<ref>PMID:17127621</ref>
| + | [https://www.uniprot.org/uniprot/BASI_HUMAN BASI_HUMAN] Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to the plasma membrane. Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes.<ref>PMID:17127621</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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Armstrong, G S]] | + | [[Category: Armstrong GS]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Eisenmesser EZ]] |
| - | [[Category: Eisenmesser, E Z]] | + | [[Category: Isern NG]] |
| - | [[Category: Isern, N G]] | + | [[Category: Kieft JS]] |
| - | [[Category: Kieft, J S]] | + | [[Category: Redzic JS]] |
| - | [[Category: Redzic, J S]] | + | |
| - | [[Category: Beta sheet]]
| + | |
| - | [[Category: Bsgc]]
| + | |
| - | [[Category: Cd147]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Emmprin]]
| + | |
| - | [[Category: Immunoglobulin-like domain]]
| + | |
| Structural highlights
Function
BASI_HUMAN Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to the plasma membrane. Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes.[1]
Publication Abstract from PubMed
CD147 is a type I transmembrane protein that is involved in inflammatory diseases, cancer progression, and multiple human pathogens utilize CD147 for efficient infection. CD147 expression is so high in several cancers that it is now used as a prognostic marker. The two primary isoforms of CD147 that are related to cancer progression have been identified, differing in their number of immunoglobulin (Ig)-like domains. These include CD147 Ig1-Ig2, which is ubiquitously expressed in most tissues, and CD147 Ig0-Ig1-Ig2, which is retinal specific and implicated in retinoblastoma. However, little is known in regard to the retinal specific CD147 Ig0 domain despite its potential role in retinoblastoma. We present the first crystal structure of the human CD147 Ig0 domain and show that the CD147 Ig0 domain is a crystallographic dimer with an I-type domain structure, which maintained in solution. Furthermore, we have utilized our structural data together with mutagenesis to probe the biological activity of CD147-containing proteins, both with and without the CD147 Ig0 domain, within several model cell lines. Our findings reveal that the CD147 Ig0 domain is a potent stimulator of interleukin-6 and suggest that the CD147 Ig0 domain has its own receptor distinct from that of the other CD147 Ig-like domains, CD147 Ig1-Ig2. Finally, we show that the CD147 Ig0 dimer is the functional unit required for activity and can be disrupted by a single point mutation.
The Retinal Specific CD147 Ig0 Domain: From Molecular Structure to Biological Activity.,Redzic JS, Armstrong GS, Isern NG, Jones DN, Kieft JS, Eisenmesser EZ J Mol Biol. 2011 Aug 5;411(1):68-82. Epub 2011 May 19. PMID:21620857[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Manoharan C, Wilson MC, Sessions RB, Halestrap AP. The role of charged residues in the transmembrane helices of monocarboxylate transporter 1 and its ancillary protein basigin in determining plasma membrane expression and catalytic activity. Mol Membr Biol. 2006 Nov-Dec;23(6):486-98. PMID:17127621 doi:http://dx.doi.org/10.1080/09687860600841967
- ↑ Redzic JS, Armstrong GS, Isern NG, Jones DN, Kieft JS, Eisenmesser EZ. The Retinal Specific CD147 Ig0 Domain: From Molecular Structure to Biological Activity. J Mol Biol. 2011 Aug 5;411(1):68-82. Epub 2011 May 19. PMID:21620857 doi:10.1016/j.jmb.2011.04.060
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