View source for 7d2u


==Crystal structure of Rsu1/PINCH1_LIM45C complex==
<StructureSection load='7d2u' size='340' side='right'caption='[[7d2u]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7d2u]] 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=7D2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D2U FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7d2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d2u OCA], [https://pdbe.org/7d2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d2u RCSB], [https://www.ebi.ac.uk/pdbsum/7d2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d2u ProSAT]</span></td></tr>
</table>
== 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Communications between actin filaments and integrin-mediated focal adhesion (FA) are crucial for cell adhesion and migration. As a core platform to organize FA proteins, the tripartite ILK/PINCH/Parvin (IPP) complex interacts with actin filaments to regulate the cytoskeleton-FA crosstalk. Rsu1, a Ras suppressor, is enriched in FA through PINCH1 and plays important roles in regulating F-actin structures. Here, we solved crystal structures of the Rsu1/PINCH1 complex, in which the leucine-rich-repeats of Rsu1 form a solenoid structure to tightly associate with the C-terminal region of PINCH1. Further structural analysis uncovered that the interaction between Rsu1 and PINCH1 blocks the IPP-mediated F-actin bundling by disrupting the binding of PINCH1 to actin. Consistently, overexpressing Rsu1 in HeLa cells impairs stress fiber formation and cell spreading. Together, our findings demonstrated that Rsu1 is critical for tuning the communication between F-actin and FA by interacting with the IPP complex and negatively modulating the F-actin bundling.

Complex structures of Rsu1 and PINCH1 reveal a regulatory mechanism of the ILK/PINCH/Parvin complex for F-actin dynamics.,Yang H, Lin L, Sun K, Zhang T, Chen W, Li L, Xie Y, Wu C, Wei Z, Yu C Elife. 2021 Feb 15;10:e64395. doi: 10.7554/eLife.64395. PMID:33587032<ref>PMID:33587032</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7d2u" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cong Y]]
[[Category: Wei Z]]
[[Category: Yang H]]