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4gmv

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==Crystal Structure of the coiled-coil, RA and PH domains of Lamellipodin==
==Crystal Structure of the coiled-coil, RA and PH domains of Lamellipodin==
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<StructureSection load='4gmv' size='340' side='right' caption='[[4gmv]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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<StructureSection load='4gmv' size='340' side='right'caption='[[4gmv]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gmv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GMV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GMV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gmv]] 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=4GMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GMV FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gn1|4gn1]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.403&#8491;</td></tr>
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<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 Homo sapiens])</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=4gmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gmv OCA], [https://pdbe.org/4gmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gmv RCSB], [https://www.ebi.ac.uk/pdbsum/4gmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gmv ProSAT]</span></td></tr>
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<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=4gmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gmv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gmv RCSB], [http://www.ebi.ac.uk/pdbsum/4gmv PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Chang, Y C.E]]
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[[Category: Large Structures]]
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[[Category: Wu, J]]
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[[Category: Chang YCE]]
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[[Category: Cell adhesion]]
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[[Category: Wu J]]
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[[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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Current revision

Crystal Structure of the coiled-coil, RA and PH domains of Lamellipodin

PDB ID 4gmv

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