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| | ==Crystal Structure of the RA and PH domains of Lamellipodin== | | ==Crystal Structure of the RA and PH domains of Lamellipodin== |
| - | <StructureSection load='4gn1' size='340' side='right' caption='[[4gn1]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4gn1' size='340' side='right'caption='[[4gn1]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gn1]] 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=4GN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GN1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gn1]] 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=4GN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GN1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gmv|4gmv]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAPH1, ALS2CR18, ALS2CR9, KIAA1681, LPD, PREL2, RMO1 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4gn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gn1 OCA], [https://pdbe.org/4gn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gn1 RCSB], [https://www.ebi.ac.uk/pdbsum/4gn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gn1 ProSAT]</span></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=4gn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gn1 OCA], [http://pdbe.org/4gn1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4gn1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gn1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RAPH1_HUMAN RAPH1_HUMAN]] Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion. | + | [https://www.uniprot.org/uniprot/RAPH1_HUMAN RAPH1_HUMAN] Mediator of localized membrane signals. Implicated in the regulation of lamellipodial dynamics. Negatively regulates cell adhesion. |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | The adapter protein Lamellipodin (Lpd) plays an important role in cell migration. In particular, Lpd mediates lamellipodia formation by regulating actin dynamics via interacting with Ena/VASP proteins. Its RA-PH tandem domain configuration suggests that like its paralog RIAM, Lpd may also mediate particular Ras GTPase signaling. We determined the crystal structures of the Lpd RA-PH domains alone and with an N-terminal coiled-coil region (cc-RA-PH). These structures reveal that apart from the anticipated coiled-coil interaction, Lpd may also oligomerize through a second intermolecular contact site. We then validated both oligomerization interfaces in solution by mutagenesis. A fluorescence-polarization study demonstrated that Lpd binds phosphoinositol with low affinity. Based on our crystallographic and biochemical data, we propose that Lpd and RIAM serve diverse functions: Lpd plays a predominant role in regulating actin polymerization, and its function in mediating Ras GTPase signaling is largely suppressed compared to RIAM.
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| - | Crystal structure of Lamellipodin implicates diverse functions in actin polymerization and Ras signaling.,Chang YC, Zhang H, Brennan ML, Wu J Protein Cell. 2013 Mar;4(3):211-9. doi: 10.1007/s13238-013-2082-5. Epub 2013 Mar , 13. PMID:23483482<ref>PMID:23483482</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4gn1" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Chang, Y C.E]] | + | [[Category: Large Structures]] |
| - | [[Category: Wu, J]] | + | [[Category: Chang YCE]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Wu J]] |
| - | [[Category: Cell migration]]
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| - | [[Category: Coiled-coil region]]
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| - | [[Category: Cytoskeletal protein]]
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| - | [[Category: Ena/vasp binding]]
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| - | [[Category: Pleckstrin homology domain]]
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| - | [[Category: Ra-ph]]
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| - | [[Category: Ras-association domain]]
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| - | [[Category: Signaling protein]]
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