6rlr

From Proteopedia

(Difference between revisions)

Revision as of 12:23, 24 January 2024

Crystal structure of CD9 large extracellular loop

Structural highlights

6rlr is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CD9_HUMAN Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion (PubMed:8478605, PubMed:14575715, PubMed:18541721). Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion (By similarity). In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (PubMed:12796480). Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). Acts as a receptor for PSG17 (By similarity). Involved in platelet activation and aggregation (PubMed:18541721). Regulates paranodal junction formation (By similarity). Involved in cell adhesion, cell motility and tumor metastasis (PubMed:8478605, PubMed:7511626).[UniProtKB:P40240]^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Tetraspanins are eukaryotic membrane proteins that contribute to a variety of signaling processes by organizing partner-receptor molecules in the plasma membrane. How tetraspanins bind and cluster partner receptors into tetraspanin-enriched microdomains is unknown. Here, we present crystal structures of the large extracellular loop of CD9 bound to nanobodies 4C8 and 4E8 and, the cryo-EM structure of 4C8-bound CD9 in complex with its partner EWI-F. CD9-EWI-F displays a tetrameric arrangement with two central EWI-F molecules, dimerized through their ectodomains, and two CD9 molecules, one bound to each EWI-F transmembrane helix through CD9-helices h3 and h4. In the crystal structures, nanobodies 4C8 and 4E8 bind CD9 at loops C and D, which is in agreement with the 4C8 conformation in the CD9-EWI-F complex. The complex varies from nearly twofold symmetric (with the two CD9 copies nearly anti-parallel) to ca. 50 degrees bent arrangements. This flexible arrangement of CD9-EWI-F with potential CD9 homo-dimerization at either end provides a "concatenation model" for forming short linear or circular assemblies, which may explain the occurrence of tetraspanin-enriched microdomains.

Implications for tetraspanin-enriched microdomain assembly based on structures of CD9 with EWI-F.,Oosterheert W, Xenaki KT, Neviani V, Pos W, Doulkeridou S, Manshande J, Pearce NM, Kroon-Batenburg LM, Lutz M, van Bergen En Henegouwen PM, Gros P Life Sci Alliance. 2020 Sep 21;3(11). pii: 3/11/e202000883. doi:, 10.26508/lsa.202000883. Print 2020 Nov. PMID:32958604^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Takeda Y, Tachibana I, Miyado K, Kobayashi M, Miyazaki T, Funakoshi T, Kimura H, Yamane H, Saito Y, Goto H, Yoneda T, Yoshida M, Kumagai T, Osaki T, Hayashi S, Kawase I, Mekada E. Tetraspanins CD9 and CD81 function to prevent the fusion of mononuclear phagocytes. J Cell Biol. 2003 Jun 9;161(5):945-56. doi: 10.1083/jcb.200212031. PMID:12796480 doi:http://dx.doi.org/10.1083/jcb.200212031
↑ Higginbottom A, Takahashi Y, Bolling L, Coonrod SA, White JM, Partridge LJ, Monk PN. Structural requirements for the inhibitory action of the CD9 large extracellular domain in sperm/oocyte binding and fusion. Biochem Biophys Res Commun. 2003 Nov 7;311(1):208-14. doi:, 10.1016/j.bbrc.2003.09.196. PMID:14575715 doi:http://dx.doi.org/10.1016/j.bbrc.2003.09.196
↑ Nakazawa Y, Sato S, Naito M, Kato Y, Mishima K, Arai H, Tsuruo T, Fujita N. Tetraspanin family member CD9 inhibits Aggrus/podoplanin-induced platelet aggregation and suppresses pulmonary metastasis. Blood. 2008 Sep 1;112(5):1730-9. doi: 10.1182/blood-2007-11-124693. Epub 2008 Jun, 9. PMID:18541721 doi:http://dx.doi.org/10.1182/blood-2007-11-124693
↑ Masellis-Smith A, Shaw AR. CD9-regulated adhesion. Anti-CD9 monoclonal antibody induce pre-B cell adhesion to bone marrow fibroblasts through de novo recognition of fibronectin. J Immunol. 1994 Mar 15;152(6):2768-77. PMID:7511626
↑ Ikeyama S, Koyama M, Yamaoko M, Sasada R, Miyake M. Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA. J Exp Med. 1993 May 1;177(5):1231-7. doi: 10.1084/jem.177.5.1231. PMID:8478605 doi:http://dx.doi.org/10.1084/jem.177.5.1231
↑ Oosterheert W, Xenaki KT, Neviani V, Pos W, Doulkeridou S, Manshande J, Pearce NM, Kroon-Batenburg LM, Lutz M, van Bergen En Henegouwen PM, Gros P. Implications for tetraspanin-enriched microdomain assembly based on structures of CD9 with EWI-F. Life Sci Alliance. 2020 Sep 21;3(11). pii: 3/11/e202000883. doi:, 10.26508/lsa.202000883. Print 2020 Nov. PMID:32958604 doi:http://dx.doi.org/10.26508/lsa.202000883

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6rlr"

@@ Line 3: / Line 3: @@
 <StructureSection load='6rlr' size='340' side='right'caption='[[6rlr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6rlr]] is a 4 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=6RLR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RLR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6rlr]] is a 4 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=6RLR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RLR FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD9, MIC3, TSPAN29, GIG2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rlr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlr OCA], [http://pdbe.org/6rlr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rlr RCSB], [http://www.ebi.ac.uk/pdbsum/6rlr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlr 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=6rlr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rlr OCA], [https://pdbe.org/6rlr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rlr RCSB], [https://www.ebi.ac.uk/pdbsum/6rlr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rlr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CD9_HUMAN CD9_HUMAN]] Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion (PubMed:8478605, PubMed:14575715, PubMed:18541721). Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion (By similarity). In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (PubMed:12796480). Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). Acts as a receptor for PSG17 (By similarity). Involved in platelet activation and aggregation (PubMed:18541721). Regulates paranodal junction formation (By similarity). Involved in cell adhesion, cell motility and tumor metastasis (PubMed:8478605, PubMed:7511626).[UniProtKB:P40240]<ref>PMID:12796480</ref> <ref>PMID:14575715</ref> <ref>PMID:18541721</ref> <ref>PMID:7511626</ref> <ref>PMID:8478605</ref>
+[https://www.uniprot.org/uniprot/CD9_HUMAN CD9_HUMAN] Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion (PubMed:8478605, PubMed:14575715, PubMed:18541721). Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion (By similarity). In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (PubMed:12796480). Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). Acts as a receptor for PSG17 (By similarity). Involved in platelet activation and aggregation (PubMed:18541721). Regulates paranodal junction formation (By similarity). Involved in cell adhesion, cell motility and tumor metastasis (PubMed:8478605, PubMed:7511626).[UniProtKB:P40240]<ref>PMID:12796480</ref> <ref>PMID:14575715</ref> <ref>PMID:18541721</ref> <ref>PMID:7511626</ref> <ref>PMID:8478605</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Gros, P]]
+[[Category: Gros P]]
-[[Category: Kroon-Batenburg, L]]
+[[Category: Kroon-Batenburg L]]
-[[Category: Lutz, M]]
+[[Category: Lutz M]]
-[[Category: Neviani, V]]
+[[Category: Neviani V]]
-[[Category: Pearce, N M]]
+[[Category: Pearce NM]]
-[[Category: Pos, W]]
+[[Category: Pos W]]
-[[Category: Schotte, R]]
+[[Category: Schotte R]]
-[[Category: Spits, H]]
+[[Category: Spits H]]
-[[Category: Cd9 antigen]]
-[[Category: Immune system]]
-[[Category: Tetraspanin]]

6rlr

From Proteopedia

Revision as of 12:23, 24 January 2024

Crystal structure of CD9 large extracellular loop

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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