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| | <StructureSection load='7lt8' size='340' side='right'caption='[[7lt8]], [[Resolution|resolution]] 1.76Å' scene=''> | | <StructureSection load='7lt8' size='340' side='right'caption='[[7lt8]], [[Resolution|resolution]] 1.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7lt8]] is a 1 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=7LT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LT8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7lt8]] is a 1 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=7LT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LT8 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;'>[[7lt9|7lt9]]</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]] 1.7600025Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RSU1, RSP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lt8 OCA], [https://pdbe.org/7lt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lt8 RCSB], [https://www.ebi.ac.uk/pdbsum/7lt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lt8 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=7lt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lt8 OCA], [https://pdbe.org/7lt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lt8 RCSB], [https://www.ebi.ac.uk/pdbsum/7lt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lt8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RSU1_HUMAN RSU1_HUMAN]] Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro.
| + | [https://www.uniprot.org/uniprot/RSU1_HUMAN RSU1_HUMAN] Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Ras suppressor-1 (Rsu-1) is a leucine-rich repeat (LRR)-containing protein that is crucial for regulating cell adhesion, and is involved in such physiological and pathological processes as focal adhesion assembly and tumor metastasis. Rsu-1 interacts with zinc-finger type multi-LIM domain-containing adaptor protein PINCH-1, known to be involved in the integrin-mediated consensus adhesome, but not with its highly homologous family member PINCH-2. However, the structural basis for and regulatory mechanisms of this specific interaction remain unclear. Here, we determined the crystal structures of Rsu-1 and its complex with the PINCH-1 LIM4-5 domains. Rsu-1 displays an arc-shaped solenoid architecture, with eight LRRs shielded by N- and C-terminal capping modules. We showed that the conserved concave surface of the Rsu-1 LRR domain binds and stabilizes the PINCH-1 LIM5 domain via salt bridge and hydrophobic interactions, while the C-terminal non-LIM region of PINCH-2 sterically disfavors Rsu-1 binding. We also showed that Rsu-1 can be assembled, via PINCH-1-binding, into a hetero-pentamer complex comprising Rsu-1, PINCH-1, ILK, Parvin, and Kindlin-2, which constitute a major consensus integrin adhesome crucial for focal adhesion assembly. Our mutagenesis and cell biological data emphasize the significance of the Rsu-1/PINCH-1 interaction in focal adhesion assembly and cell spreading, providing crucial molecular insights into Rsu-1-mediated cell adhesion with implications for disease development.
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| - | | + | |
| - | Molecular basis for Ras suppressor-1 binding to PINCH-1 in focal adhesion assembly.,Fukuda K, Lu F, Qin J J Biol Chem. 2021 Apr 20:100685. doi: 10.1016/j.jbc.2021.100685. PMID:33891945<ref>PMID:33891945</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 7lt8" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fukuda, K]] | + | [[Category: Fukuda K]] |
| - | [[Category: Qin, J]] | + | [[Category: Qin J]] |
| - | [[Category: Cell adhesion]]
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| - | [[Category: Leucine-rich repeat]]
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